6BI7: PDB entry 6BI7
Crystal structure of Rev7-WT/Rev3 as a monomer under high-salt conditions. Determined by X-ray diffraction at 2.8 Å resolution. Released 1 Aug 2018.
- Method
- X-ray diffraction
- Resolution
- 2.8 Å
- Organism
- Homo sapiens
- Chains
- 8
- Atoms
- 6,445
- Mol. weight
- 117.86 kDa
- Released
- 1 Aug 2018
Explore 6BI7 in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
6BI7 contains 38 α-helices and 38 β-strands across 8 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, 8 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 | 82-89 | 8 | 2 |
| β-strand | 94-103 | 10 | 2 |
| α-helix | 117-132 | 16 | |
| α-helix | 133-136 | 4 | |
| α-helix | 138-141 | 4 | |
| β-strand | 144-153 | 10 | 2 |
| β-strand | 171-173 | 3 | 2 |
| α-helix | 174-175 | 2 | |
| α-helix | 176-179 | 4 | |
| β-strand | 185-193 | 9 | 2 |
| β-strand | 198-205 | 8 | 2 |
Chain B: 2 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 1991-1996 | 6 | 2 |
| α-helix | 1999-2002 | 4 | |
| α-helix | 2003-2011 | 9 | |
Chain C: 9 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 13-33 | 21 | |
| α-helix | 39-41 | 3 | |
| β-strand | 42-47 | 6 | 3 |
| β-strand | 50-55 | 6 | 3 |
| α-helix | 58-76 | 19 | |
| β-strand | 82-88 | 7 | 4 |
| β-strand | 94-103 | 10 | 4 |
| α-helix | 120-132 | 13 | |
| α-helix | 133-136 | 4 | |
| α-helix | 138-140 | 3 | |
| β-strand | 145-152 | 8 | 4 |
| α-helix | 163-167 | 5 | |
| β-strand | 171-173 | 3 | 4 |
| α-helix | 174-175 | 2 | |
| α-helix | 176-179 | 4 | |
| β-strand | 185-193 | 9 | 4 |
| β-strand | 198-205 | 8 | 4 |
Chain D: 2 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 1992-1996 | 5 | 4 |
| α-helix | 1999-2002 | 4 | |
| α-helix | 2003-2011 | 9 | |
Chain E: 7 helices, 10 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 13-33 | 21 | |
| α-helix | 39-41 | 3 | |
| β-strand | 42-43 | 2 | 5 |
| β-strand | 47 | 1 | 6 |
| β-strand | 50 | 1 | 6 |
| β-strand | 54-55 | 2 | 5 |
| α-helix | 58-76 | 19 | |
| β-strand | 82-87 | 6 | 7 |
| β-strand | 97-103 | 7 | 7 |
| α-helix | 117-132 | 16 | |
| α-helix | 133-135 | 3 | |
| β-strand | 146-151 | 6 | 7 |
| β-strand | 171-173 | 3 | 7 |
| α-helix | 174-175 | 2 | |
| α-helix | 176-179 | 4 | |
| β-strand | 185-193 | 9 | 7 |
| β-strand | 198-205 | 8 | 7 |
Chain F: 2 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 1994-1996 | 3 | 7 |
| α-helix | 1999-2000 | 2 | |
| α-helix | 2003-2011 | 9 | |
Chain G: 6 helices, 8 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 13-33 | 21 | |
| α-helix | 39-41 | 3 | |
| β-strand | 42-44 | 3 | 8 |
| β-strand | 53-55 | 3 | 8 |
| α-helix | 58-76 | 19 | |
| β-strand | 82-88 | 7 | 9 |
| β-strand | 94-103 | 10 | 9 |
| α-helix | 119-132 | 14 | |
| α-helix | 133-136 | 4 | |
| β-strand | 145-150 | 6 | 9 |
| β-strand | 171-173 | 3 | 9 |
| α-helix | 174-175 | 2 | |
| β-strand | 187-193 | 7 | 9 |
| β-strand | 198-203 | 6 | 9 |
Chain H: 2 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| β-strand | 1994-1996 | 3 | 9 |
| α-helix | 1999-2002 | 4 | |
| α-helix | 2003-2011 | 9 | |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Mitotic spindle assembly checkpoint protein MAD2B | A, C, E, G | protein | 227 | Homo sapiens | Q9UI95 (AlphaFold model) |
| DNA polymerase zeta catalytic subunit | B, D, F, H | protein | 28 | Homo sapiens | O60673 |
Sequence of entity 1 (A, C, E, G), FASTA
>6BI7_1 Mitotic spindle assembly checkpoint protein MAD2B (chains A, C, E, G)
MGSSHHHHHHSQDPNSMTTLTRQDLNFGQVVADVLCEFLEVAVHLILYVREVYPVGIFQK
RKKYNVPVQMSCHPELNQYIQDTLHCVKPLLEKNDVEKVVVVILDKEHRPVEKFVFEITQ
PPLLSISSDSLLSHVEQLLRAFILKISVCDAVLDHNPPGCTFTVLVHTREAATRNMEKIQ
VIKDFPWILADEQDVHMHDPRLIPLKTMTSDILKMQLYVEERAHKGS
Sequence of entity 2 (B, D, F, H), FASTA
>6BI7_2 DNA polymerase zeta catalytic subunit (chains B, D, F, H)
MEDKKIVIMPCKCAPSRQLVQVWLQAKE
Primary citation
Rev7 dimerization is important for assembly and function of the Rev1/Pol zeta translesion synthesis complex. Rizzo, A.A., Vassel, F.M., Chatterjee, N. et al. Proc Natl Acad Sci U S A (2018) 115:E8191-E8200. DOI 10.1073/pnas.1801149115 · 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
About this viewer
MolViewer shows 6BI7 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.