6BC8: PDB entry 6BC8

Crystal structure of Rev7-R124A/Rev3-RBM2 (residues 1988-2014) complex. Determined by X-ray diffraction at 1.68 Å resolution. Released 1 Aug 2018.

Method: X-ray diffraction
Resolution: 1.68 Å
Organism: Homo sapiens
Chains: 2
Atoms: 2,032
Mol. weight: 29.69 kDa
Released: 1 Aug 2018

Explore 6BC8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6BC8 contains 15 α-helices and 14 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.

Chain A: 12 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	5	1	1
α-helix	6-8	3
α-helix	10-12	3
α-helix	13-33	21
α-helix	39-41	3
β-strand	42-47	6	2
β-strand	50-55	6	2
α-helix	58-76	19
β-strand	80-88	9	3
β-strand	94-103	10	3
β-strand	107	1	1
β-strand	113	1	4
α-helix	114	1
α-helix	119-131	13
α-helix	133-135	3
α-helix	138-141	4
β-strand	145-155	11	3
α-helix	156	1
β-strand	163-166	4	3
β-strand	169-173	5	3
α-helix	174-175	2
α-helix	176-179	4
β-strand	185-193	9	3
β-strand	194	1	4
β-strand	198-205	8	3

Chain B: 3 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	1990	1
β-strand	1991-1996	6	3
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	protein	227	Homo sapiens	Q9UI95 (AlphaFold model)
DNA polymerase zeta catalytic subunit	B	protein	28	Homo sapiens	O60673

Sequence of entity 1 (A), FASTA

>6BC8_1 Mitotic spindle assembly checkpoint protein MAD2B (chains A)
MGSSHHHHHHSQDPNSMTTLTRQDLNFGQVVADVLCEFLEVAVHLILYVREVYPVGIFQK
RKKYNVPVQMSCHPELNQYIQDTLHCVKPLLEKNDVEKVVVVILDKEHRPVEKFVFEITQ
PPLLSISSDSLLSHVEQLLAAFILKISVCDAVLDHNPPGCTFTVLVHTREAATRNMEKIQ
VIKDFPWILADEQDVHMHDPRLIPLKTMTSDILKMQLYVEERAHKGS

Sequence of entity 2 (B), FASTA

>6BC8_2 DNA polymerase zeta catalytic subunit (chains B)
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)
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
6K08 2.31 Å, Crystal structure of REV7(R124A/A135D) in complex with a Shieldin3 fragment

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