Role of Beta-hairpin motifs in the DNA duplex opening by the Rad4/XPC nucleotide excision repair complex. Determined by X-ray diffraction at 4.6 Å resolution. Released 14 Oct 2020.
Explore 6UBF in 3D Show helices and sheets RCSB PDB PDBe
6UBF contains 34 α-helices and 23 β-strands across 2 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 134-163 | 30 | |
| α-helix | 165-172 | 8 | |
| α-helix | 177-183 | 7 | |
| α-helix | 185-187 | 3 | |
| α-helix | 192-213 | 22 | |
| β-strand | 216-217 | 2 | 1 |
| α-helix | 219-220 | 2 | |
| α-helix | 230-236 | 7 | |
| α-helix | 247-257 | 11 | |
| β-strand | 259-260 | 2 | 1 |
| α-helix | 262-275 | 14 | |
| β-strand | 280-286 | 7 | 2 |
| α-helix | 288-290 | 3 | |
| α-helix | 305-309 | 5 | |
| β-strand | 315-321 | 7 | 2 |
| β-strand | 326-331 | 6 | 2 |
| β-strand | 337-339 | 3 | 2 |
| β-strand | 362-366 | 5 | 2 |
| β-strand | 372-374 | 3 | 2 |
| α-helix | 376-379 | 4 | |
| α-helix | 387-390 | 4 | |
| α-helix | 392-394 | 3 | |
| α-helix | 396-409 | 14 | |
| α-helix | 416-431 | 16 | |
| α-helix | 439-441 | 3 | |
| β-strand | 447-449 | 3 | 3 |
| α-helix | 450-452 | 3 | |
| β-strand | 457-459 | 3 | 4 |
| α-helix | 460 | 1 | |
| β-strand | 467-470 | 4 | 3 |
| β-strand | 478-483 | 6 | 3 |
| α-helix | 484-486 | 3 | |
| β-strand | 487-489 | 3 | 4 |
| β-strand | 490-491 | 2 | 5 |
| α-helix | 493-497 | 5 | |
| β-strand | 501-503 | 3 | 6 |
| β-strand | 515 | 1 | 7 |
| β-strand | 527 | 1 | 7 |
| α-helix | 528-530 | 3 | |
| β-strand | 532-533 | 2 | 5 |
| α-helix | 534-536 | 3 | |
| β-strand | 537-539 | 3 | 6 |
| α-helix | 542-545 | 4 | |
| β-strand | 559-560 | 2 | 8 |
| α-helix | 564-566 | 3 | |
| β-strand | 571-575 | 5 | 8 |
| α-helix | 579-586 | 8 | |
| β-strand | 592-594 | 3 | 8 |
| β-strand | 609-615 | 7 | 8 |
| α-helix | 616-618 | 3 | |
| α-helix | 619-627 | 9 | |
| α-helix | 629-631 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 260-271 | 12 | |
| α-helix | 273-275 | 3 | |
| α-helix | 276-286 | 11 | |
| α-helix | 290-296 | 7 | |
| α-helix | 298-307 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA repair protein RAD4 | A | protein | 531 | Saccharomyces cerevisiae | P14736 (AlphaFold model) |
| UV excision repair protein RAD23 | X | protein | 171 | Saccharomyces cerevisiae | P32628 (AlphaFold model) |
| DNA (5'-D(*TP*TP*GP*AP*CP*TP*CP*(G47)P*AP*CP*AP*TP*CP*CP*C*GP*CP*TP*AP*CP*AP*A)-3') | W | DNA | 24 | Saccharomyces cerevisiae | |
| DNA (5'-d(*ap*tp*tp*gp*tp*ap*gp*cp*gp*gp*gp*ap*tp*gp*tp*cp*gp*ap*gp*tp*cp*a)-3') | Y | DNA | 24 | Saccharomyces cerevisiae |
>6UBF_1 DNA repair protein RAD4 (chains A) GSSRAMGNEVAGVEDISVEITPSSKRNSDARRTSRNCSSNEERKRRKYFHMLYLVCLMVH GFIRNEWINSKRLSRKLSNLVPEKVFELLHPQKDEELPLRSTRKLLDGLKKCMELWQKHW KITKKYDNEGLYMRTWKEIEMSANNKRKFKTLKRSDFLRAVSKGHGDPDISVQGFVAMLR ACNVNARLIMSCQPPDFTNMKIDTSLNGNNAYKDMVKYPIFWCEVWDKFSKKWITVDPVN LKTIEQVRLHSKLAPKGVACCERNMLRYVIAYDRKYGCRDVTRRYAQWMNSKVRKRRITK DDFGEKWFRKVITALHHRKRTKIDDYEDQYFFRRDESEGIPDSVQDLKNHPYYVLEQDIK QTQIVKPGCKECGYLKVHGKVGKVLKVYAKRDIADLKSARQWYMNGRILKTGSRCKKVIK RTVGRPKGEAEEEDERLYSFEDTELYIPPLASASGEITKNTFGNIEVFAPTMIPGNCCLV ENPVAIKAARFLGVEFAPAVTSFKFPVLSGIVVAKWLREAIETAIDGIEFI
>6UBF_2 UV excision repair protein RAD23 (chains X) GSGNASSGALGTTGGATDAAQGGPPGSIGLTVEDLLSLRQVVSGNPEALAPLLENISARY PQLREHIMANPEVFVSMLLEAVGDNMQDVMEGADDMVEGEDIEVTGEAAAAGLGQGEGEG SFQVDYTPEDDQAISRLCELGFERDLVIQVYFACDKNEEAAANILFSDHAD
>6UBF_3 DNA (5'-D(*TP*TP*GP*AP*CP*TP*CP*(G47)P*AP*CP*AP*TP*CP*CP*C*GP*CP*TP*AP*CP*AP*A)-3') (chains W) TTGACTCGACATCCCCCGCTACAA
>6UBF_4 DNA (5'-D(*AP*TP*TP*GP*TP*AP*GP*CP*GP*GP*GP*AP*TP*GP*TP*CP*GP*AP*GP*TP*CP*A)-3') (chains Y) ATTGTAGCGGGGGATGTCGAGTCA
Kinetic gating mechanism of DNA damage recognition by Rad4/XPC. Chen, X., Velmurugu, Y., Zheng, G. et al. Nat Commun (2015) 6:5849. DOI 10.1038/ncomms6849 · PubMed
Other PDB entries of the same protein (UniProt P14736 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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