4GK5: Human Rev3-Rev7-Rev1-Polkappa complex
Crystal structure of human Rev3-Rev7-Rev1-Polkappa complex. Determined by X-ray diffraction at 3.21 Å resolution. Released 13 Mar 2013.
- Method
- X-ray diffraction
- Resolution
- 3.21 Å
- Organism
- Homo sapiens
- Chains
- 7
- Atoms
- 5,058
- Mol. weight
- 96.82 kDa
- Released
- 13 Mar 2013
Explore 4GK5 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
4GK5 contains 28 α-helices and 26 β-strands across 6 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: 8 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 13-33 | 21 | |
| α-helix | 39-41 | 3 | |
| β-strand | 42-47 | 6 | 1 |
| β-strand | 50-55 | 6 | 1 |
| α-helix | 58-76 | 19 | |
| β-strand | 80-88 | 9 | 2 |
| β-strand | 94-103 | 10 | 2 |
| α-helix | 115-132 | 18 | |
| α-helix | 133-135 | 3 | |
| α-helix | 138-141 | 4 | |
| β-strand | 145-152 | 8 | 2 |
| α-helix | 157-163 | 7 | |
| β-strand | 166 | 1 | 3 |
| β-strand | 169 | 1 | 3 |
| β-strand | 171-173 | 3 | 2 |
| α-helix | 176-179 | 4 | |
| β-strand | 184-192 | 9 | 2 |
| β-strand | 198-206 | 9 | 2 |
Chain B: 8 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 11-33 | 23 | |
| α-helix | 39-41 | 3 | |
| β-strand | 42-47 | 6 | 4 |
| β-strand | 50-55 | 6 | 4 |
| α-helix | 58-76 | 19 | |
| β-strand | 80-88 | 9 | 5 |
| β-strand | 94-102 | 9 | 5 |
| α-helix | 120-132 | 13 | |
| α-helix | 133-135 | 3 | |
| α-helix | 138-141 | 4 | |
| β-strand | 145-152 | 8 | 5 |
| α-helix | 157-163 | 7 | |
| β-strand | 171-173 | 3 | 5 |
| α-helix | 176-179 | 4 | |
| β-strand | 185-191 | 7 | 5 |
| β-strand | 199-205 | 7 | 5 |
Chain C: 2 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 1877-1880 | 4 | 2 |
| α-helix | 1883-1885 | 3 | |
| α-helix | 1888-1891 | 4 | |
Chain D: 2 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 1877-1880 | 4 | 5 |
| α-helix | 1883-1884 | 2 | |
| α-helix | 1887-1890 | 4 | |
Chain E: 4 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 1159 | 1 | 6 |
| β-strand | 1162 | 1 | 6 |
| α-helix | 1165-1178 | 14 | |
| α-helix | 1184-1199 | 16 | |
| α-helix | 1203-1219 | 17 | |
| α-helix | 1223-1243 | 21 | |
| β-strand | 1247-1248 | 2 | 2 |
Chain F: 4 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 1159 | 1 | 7 |
| β-strand | 1162 | 1 | 7 |
| α-helix | 1165-1177 | 13 | |
| α-helix | 1184-1199 | 16 | |
| α-helix | 1203-1216 | 14 | |
| α-helix | 1224-1243 | 20 | |
| β-strand | 1247-1248 | 2 | 5 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Mitotic spindle assembly checkpoint protein MAD2B | A, B | protein | 238 | Homo sapiens | Q9UI95 (AlphaFold model) |
| DNA polymerase zeta catalytic subunit | C, D | protein | 52 | Homo sapiens | O60673 |
| DNA repair protein REV1 | E, F | protein | 136 | Homo sapiens | Q9UBZ9 (AlphaFold model) |
| DNA polymerase kappa | G | protein | 10 | Homo sapiens | Q9UBT6 (AlphaFold model) |
Sequence of entity 1 (A, B), FASTA
>4GK5_1 Mitotic spindle assembly checkpoint protein MAD2B (chains A, B)
MGSSHHHHHHSQDPNSMTTLTRQDLNFGQVVADVLCEFLEVAVHLILYVREVYPVGIFQK
RKKYNVPVQMSCHPELNQYIQDTLHCVKPLLEKNDVEKVVVVILDKEHRPVEKFVFEITQ
PPLLSISSDSLLSHVEQLLAAFILKISVCDAVLDHNPPGCTFTVLVHTREAATRNMEKIQ
VIKDFPWILADEQDVHMHDPRLIPLKTMTSDILKMQLYVEERAHKGSGSGSGSGSGSH
Sequence of entity 2 (C, D), FASTA
>4GK5_2 DNA polymerase zeta catalytic subunit (chains C, D)
MLTPTPDSSPRSTSSPSQSKNGSFTPRTANILKPLMSPPSREEIMATLLDHD
Sequence of entity 3 (E, F), FASTA
>4GK5_3 DNA repair protein REV1 (chains E, F)
MLKHEGPPAEKPLEELSASTSGVPGLSSLQSDPAGCVRPPAPNLAGAVEFNDVKTLLREW
ITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKYMKRLMQQSVESVWNMAFDFILDN
VQVVLQQTYGSTLKVT
Sequence of entity 4 (G), FASTA
>4GK5_4 DNA polymerase kappa (chains G)
KKSFFDKKRS
Primary citation
Structural insights into the assembly of human translesion polymerase complexes. Xie, W., Yang, X., Xu, M. et al. Protein Cell (2012) 3:864-874. DOI 10.1007/s13238-012-2102-x · PubMed
Other PDB entries of the same protein (UniProt Q9UI95 (AlphaFold model), which also has an AlphaFold model), best resolution first:
- 6BCD 1.43 Å, Crystal structure of Rev7-K44A/R124A/A135D in complex with Rev3-RBM2 (residues 1988-2014)
- 6BC8 1.68 Å, Crystal structure of Rev7-R124A/Rev3-RBM2 (residues 1988-2014) complex
- 6M7B 1.77 Å, Structure of REV7-R124A complexed with SHLD3(37-73)
- 3ABD 1.9 Å, Structure of human REV7 in complex with a human REV3 fragment in a monoclinic crystal
- 4EXT 1.9 Å, Structure of polymerase-interacting domain of human Rev1 in complex with translesional…
- 6M7A 1.9 Å, Structure of REV7-R124A complexed with SHLD3(28-73)
- 6VE5 2.0 Å, X-ray structure of human REV7 in complex with Shieldin3 (residues 41-74)
- 6NIF 2.0 Å, crystal structure of human REV7-RAN complex
- 5XPT 2.1 Å, Crystal structure of MAD2L2/REV7 in complex with a CAMP fragment in a tetragonal crystal
- 6K07 2.24 Å, Crystal structure of REV7(R124A) in complex with a Shieldin3 fragment
- 6WS0 2.24 Å, Rational drug design of phenazopyridine derivatives as novel inhibitors of Rev1-CT
- 5XPU 2.3 Å, Crystal structure of MAD2L2/REV7 in complex with a CAMP fragment in a monoclinic crystal
Browse structure collections
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