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

ElementResiduesLengthSheet
α-helix13-3321
α-helix39-413
β-strand42-4761
β-strand50-5561
α-helix58-7619
β-strand82-8982
β-strand94-103102
α-helix117-13216
α-helix133-1364
α-helix138-1414
β-strand144-153102
β-strand171-17332
α-helix174-1752
α-helix176-1794
β-strand185-19392
β-strand198-20582
Chain B: 2 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand1991-199662
α-helix1999-20024
α-helix2003-20119
Chain C: 9 helices, 8 β-strands
ElementResiduesLengthSheet
α-helix13-3321
α-helix39-413
β-strand42-4763
β-strand50-5563
α-helix58-7619
β-strand82-8874
β-strand94-103104
α-helix120-13213
α-helix133-1364
α-helix138-1403
β-strand145-15284
α-helix163-1675
β-strand171-17334
α-helix174-1752
α-helix176-1794
β-strand185-19394
β-strand198-20584
Chain D: 2 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand1992-199654
α-helix1999-20024
α-helix2003-20119
Chain E: 7 helices, 10 β-strands
ElementResiduesLengthSheet
α-helix13-3321
α-helix39-413
β-strand42-4325
β-strand4716
β-strand5016
β-strand54-5525
α-helix58-7619
β-strand82-8767
β-strand97-10377
α-helix117-13216
α-helix133-1353
β-strand146-15167
β-strand171-17337
α-helix174-1752
α-helix176-1794
β-strand185-19397
β-strand198-20587
Chain F: 2 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand1994-199637
α-helix1999-20002
α-helix2003-20119
Chain G: 6 helices, 8 β-strands
ElementResiduesLengthSheet
α-helix13-3321
α-helix39-413
β-strand42-4438
β-strand53-5538
α-helix58-7619
β-strand82-8879
β-strand94-103109
α-helix119-13214
α-helix133-1364
β-strand145-15069
β-strand171-17339
α-helix174-1752
β-strand187-19379
β-strand198-20369
Chain H: 2 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand1994-199639
α-helix1999-20024
α-helix2003-20119

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Mitotic spindle assembly checkpoint protein MAD2BA, C, E, Gprotein227Homo sapiensQ9UI95 (AlphaFold model)
DNA polymerase zeta catalytic subunitB, D, F, Hprotein28Homo sapiensO60673
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:

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