8EBT: PDB entry 8EBT
XPA repositioning Core7 of TFIIH relative to XPC-DNA lesion (Cy5). Determined by electron microscopy at 3.9 Å resolution. Released 19 Apr 2023.
- Method
- Electron microscopy
- Resolution
- 3.9 Å
- Organisms
- Homo sapiens, synthetic construct
- Chains
- 12
- Atoms
- 27,026
- Mol. weight
- 423.98 kDa
- Ligands
- CA, ZN, SF4
- Released
- 19 Apr 2023
Explore 8EBT in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
8EBT contains 155 α-helices and 132 β-strands across 10 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
Chain A: 26 helices, 28 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 53 | 1 | 1 |
| β-strand | 59-60 | 2 | 1 |
| β-strand | 76-78 | 3 | 2 |
| β-strand | 84-87 | 4 | 2 |
| α-helix | 93-103 | 11 | |
| β-strand | 105-108 | 4 | 2 |
| β-strand | 113-117 | 5 | 2 |
| α-helix | 120-128 | 9 | |
| α-helix | 133-142 | 10 | |
| α-helix | 152-161 | 10 | |
| β-strand | 166-171 | 6 | 3 |
| β-strand | 174-179 | 6 | 3 |
| α-helix | 182-189 | 8 | |
| α-helix | 194-197 | 4 | |
| α-helix | 199-201 | 3 | |
| β-strand | 268-271 | 4 | 3 |
| α-helix | 277-286 | 10 | |
| β-strand | 292 | 1 | 3 |
| β-strand | 294-295 | 2 | 4 |
| α-helix | 318-327 | 10 | |
| β-strand | 328 | 1 | 4 |
| β-strand | 330 | 1 | 5 |
| β-strand | 333-334 | 2 | 4 |
| β-strand | 336-339 | 4 | 6 |
| α-helix | 347-357 | 11 | |
| β-strand | 362-365 | 4 | 6 |
| α-helix | 370-381 | 12 | |
| β-strand | 390-392 | 3 | 6 |
| β-strand | 406-409 | 4 | 6 |
| α-helix | 421-430 | 10 | |
| β-strand | 438-441 | 4 | 6 |
| α-helix | 443-445 | 3 | |
| α-helix | 452-457 | 6 | |
| β-strand | 463-467 | 5 | 6 |
| α-helix | 480-483 | 4 | |
| β-strand | 487-490 | 4 | 6 |
| α-helix | 493-498 | 6 | |
| β-strand | 505-512 | 8 | 7 |
| α-helix | 513-515 | 3 | |
| α-helix | 516-524 | 9 | |
| α-helix | 531-535 | 5 | |
| α-helix | 538-553 | 16 | |
| β-strand | 558-562 | 5 | 7 |
| α-helix | 565-573 | 9 | |
| β-strand | 579-580 | 2 | 7 |
| α-helix | 587-597 | 11 | |
| β-strand | 604-607 | 4 | 7 |
| β-strand | 622-626 | 5 | 7 |
| α-helix | 633-641 | 9 | |
| β-strand | 657-664 | 8 | 7 |
| α-helix | 668-676 | 9 | |
| α-helix | 678-682 | 5 | |
| β-strand | 688-690 | 3 | 7 |
| α-helix | 706-716 | 11 | |
Chain B: 35 helices, 24 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-5 | 4 | 8 |
| β-strand | 8-11 | 4 | 8 |
| α-helix | 19-34 | 16 | |
| β-strand | 38-41 | 4 | 9 |
| α-helix | 48-62 | 15 | |
| β-strand | 69-73 | 5 | 9 |
| β-strand | 74 | 1 | 10 |
| α-helix | 77-98 | 22 | |
| β-strand | 106-108 | 3 | 9 |
| α-helix | 130-137 | 8 | |
| α-helix | 140-145 | 6 | |
| α-helix | 157-164 | 8 | |
| α-helix | 177-187 | 11 | |
| α-helix | 191-198 | 8 | |
| β-strand | 204-206 | 3 | 9 |
| β-strand | 208 | 1 | 10 |
| α-helix | 210-213 | 4 | |
| α-helix | 215-221 | 7 | |
| β-strand | 229-233 | 5 | 9 |
| α-helix | 239-246 | 8 | |
| β-strand | 249-251 | 3 | 11 |
| α-helix | 253-271 | 19 | |
| α-helix | 327-330 | 4 | |
| α-helix | 336-340 | 5 | |
| α-helix | 342-345 | 4 | |
| α-helix | 354-364 | 11 | |
| α-helix | 370-373 | 4 | |
| α-helix | 375-386 | 12 | |
| α-helix | 395-409 | 15 | |
| β-strand | 414 | 1 | 12 |
| β-strand | 417-419 | 3 | 11 |
| β-strand | 432-435 | 4 | 11 |
| β-strand | 437 | 1 | 12 |
| α-helix | 445-450 | 6 | |
| β-strand | 455-458 | 4 | 9 |
| α-helix | 467-470 | 4 | |
| β-strand | 490-495 | 6 | 13 |
| β-strand | 497 | 1 | 14 |
| β-strand | 503 | 1 | 14 |
| α-helix | 508-510 | 3 | |
| α-helix | 514-527 | 14 | |
| β-strand | 535-539 | 5 | 13 |
| α-helix | 542-554 | 13 | |
| α-helix | 558-564 | 7 | |
| β-strand | 566-569 | 4 | 13 |
| α-helix | 574-589 | 16 | |
| β-strand | 594-599 | 6 | 13 |
| α-helix | 603-607 | 5 | |
| β-strand | 617-620 | 4 | 13 |
| α-helix | 629-631 | 3 | |
| α-helix | 633-643 | 11 | |
| α-helix | 648-664 | 17 | |
| α-helix | 665-667 | 3 | |
| β-strand | 675-680 | 6 | 13 |
| α-helix | 682-685 | 4 | |
| α-helix | 687-690 | 4 | |
| α-helix | 695-698 | 4 | |
| β-strand | 708 | 1 | 13 |
| α-helix | 710-724 | 15 | |
Chain C: 12 helices, 0 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 112-120 | 9 | |
| α-helix | 122-128 | 7 | |
| α-helix | 129-133 | 5 | |
| α-helix | 139-146 | 8 | |
| α-helix | 399-412 | 14 | |
| α-helix | 419-421 | 3 | |
| α-helix | 424-434 | 11 | |
| α-helix | 455-478 | 24 | |
| α-helix | 484-500 | 17 | |
| α-helix | 501-505 | 5 | |
| α-helix | 506-515 | 10 | |
| α-helix | 521-546 | 26 | |
Chain D: 23 helices, 18 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 19-24 | 6 | |
| α-helix | 28-34 | 7 | |
| α-helix | 38-47 | 10 | |
| α-helix | 50-58 | 9 | |
| β-strand | 66-67 | 2 | 15 |
| α-helix | 68-72 | 5 | |
| β-strand | 75 | 1 | 16 |
| α-helix | 80-93 | 14 | |
| β-strand | 96-100 | 5 | 15 |
| β-strand | 106-110 | 5 | 15 |
| α-helix | 112-122 | 11 | |
| α-helix | 145-164 | 20 | |
| α-helix | 173-182 | 10 | |
| β-strand | 185-186 | 2 | 17 |
| α-helix | 193-194 | 2 | |
| β-strand | 195-196 | 2 | 17 |
| α-helix | 198-205 | 8 | |
| α-helix | 208-226 | 19 | |
| α-helix | 230-241 | 12 | |
| α-helix | 243-244 | 2 | |
| β-strand | 249-250 | 2 | 18 |
| α-helix | 256-268 | 13 | |
| β-strand | 271-272 | 2 | 19 |
| β-strand | 280-281 | 2 | 18 |
| β-strand | 282-283 | 2 | 19 |
| α-helix | 285-289 | 5 | |
| β-strand | 307-310 | 4 | 1 |
| β-strand | 314-317 | 4 | 1 |
| α-helix | 322-331 | 10 | |
| β-strand | 333-338 | 6 | 1 |
| β-strand | 341-345 | 5 | 1 |
| α-helix | 348-357 | 10 | |
| α-helix | 361-370 | 10 | |
| β-strand | 372 | 1 | 1 |
| α-helix | 376-378 | 3 | |
| α-helix | 385-398 | 14 | |
| β-strand | 402-409 | 8 | 20 |
| α-helix | 415-428 | 14 | |
| β-strand | 431-435 | 5 | 20 |
| β-strand | 440-443 | 4 | 20 |
| α-helix | 445-461 | 17 | |
Chain E: 19 helices, 17 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 14 | 1 | 5 |
| α-helix | 15-16 | 2 | |
| α-helix | 18-21 | 4 | |
| α-helix | 30-41 | 12 | |
| β-strand | 59-66 | 8 | 21 |
| α-helix | 69-72 | 4 | |
| α-helix | 80-98 | 19 | |
| β-strand | 103-110 | 8 | 21 |
| β-strand | 113-121 | 9 | 21 |
| α-helix | 124-135 | 12 | |
| α-helix | 145-157 | 13 | |
| β-strand | 164-170 | 7 | 21 |
| α-helix | 182-191 | 10 | |
| β-strand | 195-200 | 6 | 21 |
| α-helix | 206-215 | 10 | |
| β-strand | 219-221 | 3 | 21 |
| α-helix | 225-236 | 12 | |
| α-helix | 238-240 | 3 | |
| β-strand | 249-253 | 5 | 22 |
| β-strand | 257-258 | 2 | 23 |
| α-helix | 273-276 | 4 | |
| α-helix | 281-282 | 2 | |
| β-strand | 288-290 | 3 | 23 |
| β-strand | 297-298 | 2 | 23 |
| β-strand | 311-312 | 2 | 22 |
| α-helix | 315-319 | 5 | |
| α-helix | 322-325 | 4 | |
| α-helix | 327-331 | 5 | |
| β-strand | 332-335 | 4 | 24 |
| β-strand | 344 | 1 | 25 |
| β-strand | 351 | 1 | 25 |
| β-strand | 356-359 | 4 | 24 |
| β-strand | 366-367 | 2 | 24 |
| α-helix | 369-374 | 6 | |
| α-helix | 375-379 | 5 | |
| α-helix | 383-386 | 4 | |
Chain F: 11 helices, 12 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 7-16 | 10 | 26 |
| α-helix | 19-27 | 9 | |
| α-helix | 34-51 | 18 | |
| β-strand | 56-62 | 7 | 26 |
| β-strand | 67-69 | 3 | 26 |
| α-helix | 102-120 | 19 | |
| α-helix | 133-150 | 18 | |
| β-strand | 156-165 | 10 | 26 |
| α-helix | 174-186 | 13 | |
| β-strand | 190-195 | 6 | 26 |
| α-helix | 201-210 | 10 | |
| β-strand | 214-216 | 3 | 26 |
| α-helix | 220-222 | 3 | |
| α-helix | 223-227 | 5 | |
| α-helix | 235-240 | 6 | |
| β-strand | 241 | 1 | 16 |
| α-helix | 244-247 | 4 | |
| β-strand | 249 | 1 | 23 |
| β-strand | 253-254 | 2 | 27 |
| β-strand | 261-262 | 2 | 27 |
| β-strand | 264-268 | 5 | 22 |
| β-strand | 274-275 | 2 | 22 |
| α-helix | 283-287 | 5 | |
Chain G: 3 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 5-11 | 7 | 20 |
| α-helix | 14-26 | 13 | |
| β-strand | 36-37 | 2 | 20 |
| β-strand | 42-45 | 4 | 20 |
| α-helix | 47-49 | 3 | |
| α-helix | 50-63 | 14 | |
Chain H: 15 helices, 20 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 649 | 1 | 28 |
| β-strand | 658 | 1 | 29 |
| β-strand | 669-670 | 2 | 30 |
| β-strand | 673-674 | 2 | 30 |
| β-strand | 675 | 1 | 28 |
| α-helix | 678-680 | 3 | |
| β-strand | 682 | 1 | 29 |
| β-strand | 685 | 1 | 31 |
| α-helix | 687-692 | 6 | |
| β-strand | 695-697 | 3 | 32 |
| α-helix | 698 | 1 | |
| α-helix | 701-703 | 3 | |
| β-strand | 705-707 | 3 | 33 |
| α-helix | 712-720 | 9 | |
| α-helix | 723-727 | 5 | |
| β-strand | 730-732 | 3 | 33 |
| β-strand | 733 | 1 | 31 |
| β-strand | 738-740 | 3 | 32 |
| α-helix | 741 | 1 | |
| β-strand | 745 | 1 | 34 |
| β-strand | 747 | 1 | 35 |
| β-strand | 750 | 1 | 35 |
| β-strand | 759-760 | 2 | 36 |
| α-helix | 764-766 | 3 | |
| α-helix | 768 | 1 | |
| β-strand | 769 | 1 | 34 |
| β-strand | 771-774 | 4 | 36 |
| α-helix | 779-785 | 7 | |
| β-strand | 791-799 | 9 | 36 |
| β-strand | 804-814 | 11 | 36 |
| α-helix | 819-864 | 46 | |
| α-helix | 890-901 | 12 | |
| α-helix | 904-914 | 11 | |
| α-helix | 927-933 | 7 | |
| α-helix | 936-938 | 3 | |
2 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| General transcription and DNA repair factor IIH helicase subunit XPB | A | protein | 603 | Homo sapiens | P19447 (AlphaFold model) |
| General transcription and DNA repair factor IIH helicase subunit XPD | B | protein | 730 | Homo sapiens | P18074 (AlphaFold model) |
| General transcription factor IIH subunit 1 | C | protein | 438 | Homo sapiens | P32780 (AlphaFold model) |
| General transcription factor IIH subunit 4 | D | protein | 446 | Homo sapiens | Q92759 (AlphaFold model) |
| General transcription factor IIH subunit 2 | E | protein | 380 | Homo sapiens | Q13888 |
| General transcription factor IIH subunit 3 | F | protein | 284 | Homo sapiens | Q13889 |
| General transcription factor IIH subunit 5 | G | protein | 66 | Homo sapiens | Q6ZYL4 |
| DNA repair protein complementing XP-C cells | H | protein | 274 | Homo sapiens | Q01831 |
| Centrin-2 | J | protein | 70 | Homo sapiens | P41208 |
| DNA repair protein complementing XP-A cells | K | protein | 172 | Homo sapiens | P23025 |
| DNA (Cy5) | L | DNA | 44 | synthetic construct | |
| DNA | M | DNA | 45 | synthetic construct | |
Sequence of entity 1 (A), FASTA
>8EBT_1 General transcription and DNA repair factor IIH helicase subunit XPB (chains A)
KVDEYGAKDYRLQMPLKDDHTSRPLWVAPDGHIFLEAFSPVYKYAQDFLVAIAEPVCRPT
HVHEYKLTAYSLYAAVSVGLQTSDITEYLRKLSKTGVPDGIMQFIKLCTVSYGKVKLVLK
HNRYFVESCHPDVIQHLLQDPVIRECRLRNSEGEATETVSFEVKQEMIEELQKRCIHLEY
PLLAEYDFRNDSVNPDINIDLKPTAVLRPYQEKSLRKMFGNGRARSGVIVLPCGAGKSLV
GVTAACTVRKRCLVLGNSAVSVEQWKAQFKMWSTIDDSQICRFTSDAKDKPIGCSVAIST
YSMLGHTTKRSWEAERVMEWLKTQEWGLMILDEVHTIPAKMFRRVLTIVQAHCKLGLTAT
LVREDDKIVDLNFLIGPKLYEANWMELQNNGYIAKVQCAEVWCPMSPEFYREYVAIKTKK
RILLYTMNPNKFRACQFLIKFHERRNDKIIVFADNVFALKEYAIRLNKPYIYGPTSQGER
MQILQNFKHNPKINTIFISKVGDTSFDLPEANVLIQISSHGGSRRQEAQRLGRVLRYNAF
FYSLVSQDTQEMAYSTKRQRFLVDQGYSFKVITKLAGMEEEDLAFSTKEEQQQLLQKVLA
ATD
Sequence of entity 2 (B), FASTA
>8EBT_2 General transcription and DNA repair factor IIH helicase subunit XPD (chains B)
MKLNVDGLLVYFPYDYIYPEQFSYMRELKRTLDAKGHGVLEMPSGTGKTVSLLALIMAYQ
RAYPLEVTKLIYCSRTVPEIEKVIEELRKLLNFYEKQEGEKLPFLGLALSSRKNLCIHPE
VTPLRFGKDVDGKCHSLTASYVRAQYQHDTSLPHCRFYEEFDAHGREVPLPAGIYNLDDL
KALGRRQGWCPYFLARYSILHANVVVYSYHYLLDPKIADLVSKELARKAVVVFDEAHNID
NVCIDSMSVNLTRRTLDRCQGNLETLQKTVLRIKETDEQRLRDEYRRLVEGLREASAARE
TDAHLANPVLPDEVLQEAVPGSIRTAEHFLGFLRRLLEYVKWRLRVQHVVQESPPAFLSG
LAQRVCIQRKPLRFCAERLRSLLHTLEITDLADFSPLTLLANFATLVSTYAKGFTIIIEP
FDDRTPTIANPILHFSCMDASLAIKPVFERFQSVIITSGTLSPLDIYPKILDFHPVTMAT
FTMTLARVCLCPMIIGRGNDQVAISSKFETREDIAVIRNYGNLLLEMSAVVPDGIVAFFT
SYQYMESTVASWYEQGILENIQRNKLLFIETQDGAETSVALEKYQEACENGRGAILLSVA
RGKVSEGIDFVHHYGRAVIMFGVPYVYTQSRILKARLEYLRDQFQIRENDFLTFDAMRHA
AQCVGRAIRGKTDYGLMVFADKRFARGDKRGKLPRWIQEHLTDANLNLTVDEGVQVAKYF
LRQMAQPFHR
Sequence of entity 3 (C), FASTA
>8EBT_3 General transcription factor IIH subunit 1 (chains C)
LEEKNRMLQEDPVLFQLYKDLVVSQVISAEEFWANRLNVNATDSSSTSNHKQDVGISAAF
LADVRPQTDGCNGLRYNLTSDIIESIFRTYPAVKMKYAENVPHNMTEKEFWTRFFQSHYF
HRDRLNTGSKDLFAECAKIDEKGLKTMVSLGVKNPLLDLTALEDKPLDEGYGISSVPSAS
NSKSIKENSNAAIIKRFNHHSAMVLAAGLRKQEAQNEQTSEPSNMDGNSGDADCFQPAVK
RAKLQESIEYEDLGKNNSVKTIALNLKKSDRYYHGPTPIQSLQYATSQDIINSFQSIRQE
MEAYTPKLTQVLSSSAASSTITALSPGGALMQGGTQQAINQMVPNDIQSELKHLYVAVGE
LLRHFWSCFPVNTPFLEEKVVKMKSNLERFQVTKLCPFQEKIRRQYLSTNLVSHIEEMLQ
TAYNKLHTWQSRRLMKKT
Sequence of entity 4 (D), FASTA
>8EBT_4 General transcription factor IIH subunit 4 (chains D)
RNLQEFLGGLSPGVLDRLYGHPATCLAVFRELPSLAKNWVMRMLFLEQPLPQAAVALWVK
KEFSKAQEESTGLLSGLRIWHTQLLPGGLQGLILNPIFRQNLRIALLGGGKAWSDDTSQL
GPDKHARDVPSLDKYAEERWEVVLHFMVGSPSAAVSQDLAQLLSQAGLMKSTEPGEPPCI
TSAGFQFLLLDTPAQLWYFMLQYLQTAQSRGMDLVEILSFLFQLSFSTLGKDYSVEGMSD
SLLNFLQHLREFGLVFQRKRKSRRYYPTRLAINLSSGVSGAGGTVHQPGFIVVETNYRLY
AYTESELQIALIALFSEMLYRFPNMVVAQVTRESVQQAIASGITAQQIIHFLRTRAHPVM
LKQTPVLPPTITDQIRLWELERDRLRFTEGVLYNQFLSQVDFELLLAHARELGVLVFENS
AKRLMVVTPAGHSDVKRFWKRQKHSS
Sequence of entity 5 (E), FASTA
>8EBT_5 General transcription factor IIH subunit 2 (chains E)
TKRWEGGYERTWEILKEDESGSLKATIEDILFKAKRKRVFEHHGGVRLGMMRHLYVVVDG
SRTMEDQDLKPNRLTCTLKLLEYFVEEYFDQNPISQIGIIVTKSKRAEKLTELSGNPRKH
ITSLKKAVDMTCHGEPSLYNSLSIAMQTLKHMPGHTSREVLIIFSSLTTCDPSNIYDLIK
TLKAAKIRVSVIGLSAEVRVCTVLARETGGTYHVILDESHYKELLTHHVSPPPASSSSEC
SLIRMGFPQHTIASLSDQDAKPSFSMAHLDGNTEPGLTLGGYFCPQCRAKYCELPVECKI
CGLTLVSAPHLARSYHHLFPLDAFQEIPLEEYNGERFCYGCQGELKDQHVYVCAVCQNVF
CVDCDVFVHDSLHCCPGCIH
Sequence of entity 6 (F), FASTA
>8EBT_6 General transcription factor IIH subunit 3 (chains F)
DELNLLVIVVDANPIWWGKQALKESQFTLSKCIDAVMVLGNSHLFMNRSNKLAVIASHIQ
ESRFLYPGKNGRLGDFFGDPGNPPEFNPSGSKDGKYELLTSANEVIVEEIKDLMTKSDIK
GQHTETLLAGSLAKALCYIHRMNKEVKDNQEMKSRILVIKAAEDSALQYMNFMNVIFAAQ
KQNILIDACVLDSDSGLLQQACDITGGLYLKVPQMPSLLQYLLWVFLPDQDQRSQLILPP
PVHVDYRAACFCHRNLIEIGYVCSVCLSIFCNFSPICTTCETAF
Sequence of entity 7 (G), FASTA
>8EBT_7 General transcription factor IIH subunit 5 (chains G)
VLKGVLIECDPAMKQFLLYLDESNALGKKFIIQDIDDTHVFVIAELVNVLQERVGELMDQ
NAFSLT
Sequence of entity 8 (H), FASTA
>8EBT_8 DNA repair protein complementing XP-C cells (chains H)
PTAIGLYKNHPLYALKRHLLKYEAIYPETAAILGYCRGEAVYSRDCVHTLHSRDTWLKKA
RVVRLGEVPYKMVKGFSNRARKARLAEPQLREENDLGLFGYWQTEEYQPPVAVDGKVPRN
EFGNVYLFLPSMMPIGCVQLNLPNLHRVARKLDIDCVQAITGFDFHGGYSHPVTDGYIVC
EEFKDVLLTAWENEQAVIERKEKEKKEKRALGNWKLLAKGLLIRERLKRRYGGTSSQAEA
ARILAASWPQNREDEEKQKEKKAAASHLFPFEKL
Sequence of entity 9 (J), FASTA
>8EBT_9 Centrin-2 (chains J)
KEEILKAFKLFDDDETGKISFKNLKRVAKELGENLTDEELQEMIDEADRDGDGEVSEQEF
LRIMKKTSLY
Sequence of entity 10 (K), FASTA
>8EBT_10 DNA repair protein complementing XP-A cells (chains K)
YVICEECGKEFMDSYLMNHFDLPTCDNCRDADDKHKLITKTEAKQEYLLKDCDLEKREPP
LKFIVKKNPHHSQWGDMKLYLKLQIVKRSLEVWGSQEALEEAKEVRQENREKMKQKKFDK
KVKELRRAVRSSVWKRETIVHQHEYGPEENLEDDMYRKTCTMCGHELTYEKM
Sequence of entity 11 (L), FASTA
>8EBT_11 DNA (Cy5) (chains L)
AGGTAGTCACAGCTGATTGCGCTGAGGATXTAGACGTGCGATAT
Sequence of entity 12 (M), FASTA
>8EBT_12 DNA (chains M)
ATATCGCACGTCTATTATCCTCAGCGCAATCAGCTGTGACTACCT
Ligands and cofactors
| ID | Name | Formula | Copies |
|---|
| CA | Calcium ion | Ca | 2 |
| ZN | Zinc ion | Zn | 6 |
| SF4 | Iron/sulfur cluster | Fe4 S4 | 1 |
Primary citation
Lesion recognition by XPC, TFIIH and XPA in DNA excision repair. Kim, J., Li, C.L., Chen, X. et al. Nature (2023) 617:170-175. DOI 10.1038/s41586-023-05959-z · PubMed
Other PDB entries of the same protein (UniProt P19447 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 4ERN 1.8 Å, Crystal structure of the C-terminal domain of human XPB/ERCC-3 excision repair protein…
- 7NVV 2.9 Å, XPB-containing part of TFIIH in a post-translocated state (with ADP-BeF3)
- 28JM 3.29 Å, Cryo-EM structure of the human holo-TFIIH and XPC initial encounter complex
- 7EGB 3.3 Å, TFIID-based holo PIC on SCP promoter
- 8EBU 3.3 Å, XPC release from Core7-XPA-DNA (Cy5)
- 9PD3 3.3 Å, NER dual incision complex - DuIS
- 28JS 3.32 Å, Cryo-EM structure of the human holo-TFIIH-XPC complex bound to bulky lesion-mimic DNA…
- 9PD4 3.4 Å, NER dual incision complex - DuIM
- 6RO4 3.5 Å, Structure of the core TFIIH-XPA-DNA complex
- 7AD8 3.5 Å, Core TFIIH-XPA-DNA complex with modelled p62 subunit
- 9XYU 3.5 Å, NER complex - C7CAD.ATP
- 28KE 3.6 Å, Cryo-EM structure of the human holo-TFIIH-XPC-XPA complex bound to bulky lesion-mimic DNA
Browse structure collections
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