Crystal structure of Rad4-Rad23 bound to a 6-4 photoproduct UV lesion. Determined by X-ray diffraction at 3.36 Å resolution. Released 27 Feb 2019.
Explore 6CFI in 3D Show helices and sheets RCSB PDB PDBe
6CFI contains 36 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 | 134-162 | 29 | |
| α-helix | 165-172 | 8 | |
| α-helix | 177-183 | 7 | |
| α-helix | 185-187 | 3 | |
| α-helix | 192-214 | 23 | |
| β-strand | 216-217 | 2 | 1 |
| α-helix | 218-220 | 3 | |
| α-helix | 227-229 | 3 | |
| α-helix | 230-238 | 9 | |
| α-helix | 248-257 | 10 | |
| β-strand | 259-260 | 2 | 1 |
| α-helix | 262-275 | 14 | |
| β-strand | 280-286 | 7 | 2 |
| α-helix | 305-309 | 5 | |
| β-strand | 315-321 | 7 | 2 |
| β-strand | 326-331 | 6 | 2 |
| β-strand | 337-339 | 3 | 2 |
| α-helix | 354-356 | 3 | |
| 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 | 416-432 | 17 | |
| 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 | 491 | 1 | 5 |
| α-helix | 493-498 | 6 | |
| β-strand | 501-503 | 3 | 6 |
| α-helix | 504 | 1 | |
| β-strand | 511-513 | 3 | 7 |
| β-strand | 529-531 | 3 | 7 |
| β-strand | 532 | 1 | 5 |
| α-helix | 534-536 | 3 | |
| β-strand | 537-539 | 3 | 6 |
| α-helix | 542-546 | 5 | |
| α-helix | 550-552 | 3 | |
| β-strand | 559-560 | 2 | 8 |
| α-helix | 564-566 | 3 | |
| β-strand | 571-575 | 5 | 8 |
| α-helix | 579-586 | 8 | |
| β-strand | 590-599 | 10 | 8 |
| β-strand | 605-615 | 11 | 8 |
| α-helix | 616-618 | 3 | |
| α-helix | 619-627 | 9 | |
| α-helix | 629-631 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 259-271 | 13 | |
| α-helix | 273-275 | 3 | |
| α-helix | 276-286 | 11 | |
| α-helix | 290-296 | 7 | |
| α-helix | 298-306 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| DNA repair protein RAD4 | A | protein | 538 | Saccharomyces cerevisiae S288c | P14736 (AlphaFold model) |
| UV excision repair protein RAD23 | X | protein | 171 | Saccharomyces cerevisiae S288c | P32628 (AlphaFold model) |
| DNA('-d(*tp*tp*gp*ap*cp*tp*cp*ap*ap*cp*ap*tp*cp*cp*ap*ap*ap*gp*cp*tp*ap*cp*ap*a)-') | W | DNA | 24 | synthetic construct | |
| DNA (5'-D(*AP*TP*TP*GP*TP*AP*GP*CP*(T64)P*TP*GP*GP*AP*TP*GP*TP*TP*GP*AP*GP*TP*CP*A)-3') | Y | DNA | 23 | synthetic construct |
>6CFI_1 DNA repair protein RAD4 (chains A) GSSRAMGNEVAGVEDISVEITPSSKRNSDARRTSRNVCSNEERKRRKYFHMLYLVCLMVH GFIRNEWINSKRLSRKLSNLVPEKVFELLHPQKDEELPLRSTRKLLDGLKKCMELWQKHW KITKKYDNEGLYMRTWKEIEMSANNKRKFKTLKRSDFLRAVSKGHGDPDISVQGFVAMLR ACNVNARLIMSCQPPDFTNMKIDTSLNGNNAYKDMVKYPIFWCEVWDKFSKKWITVDPVN LKTIEQVRLHSKLAPKGVACCERNMLRYVIAYDRKYGCRDVTRRYAQWMNSKVRKRRITK DDFGEKWFRKVITALHHRKRTKIDDYEDQYFFRRDESEGIPDSVQDLKNHPYYVLEQDIK QTQIVKPGCKECGYLKVHGKVGKVLKVYAKRDIADLKSARQWYMNGRILKTGSRCKKVIK RTVGRPKGEAEEEDERLYSFEDTELYIPPLASASGEITKNTFGNIEVFAPTMIPGNCCLV ENPVAIKAARFLGVEFAPAVTSFKFERGSTVKPVLSGIVVAKWLREAIETAIDGIEFI
>6CFI_2 UV excision repair protein RAD23 (chains X) GSGNASSGALGTTGGATDAAQGGPPGSIGLTVEDLLSLRQVVSGNPEALAPLLENISARY PQLREHIMANPEVFVSMLLEAVGDNMQDVMEGADDMVEGEDIEVTGEAAAAGLGQGEGEG SFQVDYTPEDDQAISRLCELGFERDLVIQVYFACDKNEEAAANILFSDHAD
>6CFI_3 DNA('-D(*TP*TP*GP*AP*CP*TP*CP*AP*AP*CP*AP*TP*CP*CP*AP*AP*AP*GP*CP*TP*AP*CP*AP*A)-') (chains W)
TTGACTCAACATCCAAAGCTACAA>6CFI_4 DNA (5'-D(*AP*TP*TP*GP*TP*AP*GP*CP*(T64)P*TP*GP*GP*AP*TP*GP*TP*TP*GP*AP*GP*TP*CP*A)-3') (chains Y) ATTGTAGCXTGGATGTTGAGTCA
Structure and mechanism of pyrimidine-pyrimidone (6-4) photoproduct recognition by the Rad4/XPC nucleotide excision repair complex. Paul, D., Mu, H., Zhao, H. et al. Nucleic Acids Res (2019) 47:6015-6028. DOI 10.1093/nar/gkz359 · 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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