3ABE: Human REV7

Structure of human REV7 in complex with a human REV3 fragment in a tetragonal crystal. Determined by X-ray diffraction at 2.6 Å resolution. Released 16 Feb 2010.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Homo sapiens
Chains: 2
Atoms: 1,760
Mol. weight: 31.73 kDa
Released: 16 Feb 2010

Explore 3ABE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3ABE contains 11 α-helices and 9 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 C: 9 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	12-33	22
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	114-122	9
α-helix	124-132	9
α-helix	133-135	3
α-helix	138-141	4
β-strand	145-152	8	2
α-helix	158-162	5
β-strand	171-173	3	2
α-helix	176-179	4
β-strand	186-193	8	2
β-strand	198-205	8	2

Chain Z: 2 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	1877-1880	4	2
α-helix	1883-1884	2
α-helix	1887-1891	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Mitotic spindle assembly checkpoint protein MAD2B	C	protein	227	Homo sapiens	Q9UI95 (AlphaFold model)
DNA polymerase zeta catalytic subunit	Z	protein	52	Homo sapiens	O60673

Sequence of entity 1 (C), FASTA

>3ABE_1 Mitotic spindle assembly checkpoint protein MAD2B (chains C)
MGSSHHHHHHSQDPNSMTTLTRQDLNFGQVVADVLCEFLEVAVHLILYVREVYPVGIFQK
RKKYNVPVQMSCHPELNQYIQDTLHCVKPLLEKNDVEKVVVVILDKEHRPVEKFVFEITQ
PPLLSISSDSLLSHVEQLLAAFILKISVCDAVLDHNPPGCTFTVLVHTREAATRNMEKIQ
VIKDFPWILADEQDVHMHDPRLIPLKTMTSDILKMQLYVEERAHKGS

Sequence of entity 2 (Z), FASTA

>3ABE_2 DNA polymerase zeta catalytic subunit (chains Z)
MLTPTPDSSPRSTSSPSQSKNGSFTPRTANILKPLMSPPSREEIMATLLDHD

Primary citation

Crystal structure of human REV7 in complex with a human REV3 fragment and structural implication of the interaction between DNA polymerase {zeta} and REV1. Hara, K., Hashimoto, H., Murakumo, Y. et al. J Biol Chem (2010) 285:12299-12307. DOI 10.1074/jbc.M109.092403 · 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

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