4EXT: Polymerase-interacting domain of human Rev1

Structure of polymerase-interacting domain of human Rev1 in complex with translesional synthesis polymerase zeta. Determined by X-ray diffraction at 1.9 Å resolution. Released 8 May 2013.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Homo sapiens
Chains: 3
Atoms: 2,685
Mol. weight: 37.33 kDa
Released: 8 May 2013

Explore 4EXT in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4EXT contains 13 α-helices and 12 β-strands across 3 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: 4 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	159	1	1
β-strand	162	1	1
α-helix	165-178	14
α-helix	184-199	16
α-helix	203-218	16
α-helix	223-243	21
β-strand	247-248	2	2

Chain B: 2 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	877-880	4	2
α-helix	883-886	4
α-helix	887-890	4

Chain C: 7 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	14-33	20
α-helix	39-41	3
β-strand	42-47	6	3
β-strand	50-55	6	3
α-helix	58-76	19
β-strand	80-88	9	2
β-strand	94-103	10	2
α-helix	114-132	19
α-helix	138-141	4
β-strand	145-152	8	2
α-helix	157-163	7
β-strand	171-173	3	2
α-helix	176-179	4
β-strand	184-192	9	2
β-strand	198-206	9	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
DNA repair protein REV1	A	protein	96	Homo sapiens	Q9UBZ9 (AlphaFold model)
peptide from DNA polymerase zeta catalytic subunit	B	protein	23	Homo sapiens	O60673
Mitotic spindle assembly checkpoint protein MAD2B	C	protein	204	Homo sapiens	Q9UI95 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4EXT_1 DNA repair protein REV1 (chains A)
APNLAGAVEFNDVKTLLREWITTISDPMEEDILQVVKYCTDLIEEKDLEKLDLVIKYMKR
LMQQSVESVWNMAFDFILDNVQVVLQQTYGSTLKVT

Sequence of entity 2 (B), FASTA

>4EXT_2 peptide from DNA polymerase zeta catalytic subunit (chains B)
RTANILKPLMSPPSREEIMATLL

Sequence of entity 3 (C), FASTA

>4EXT_3 Mitotic spindle assembly checkpoint protein MAD2B (chains C)
TQDLNFGQVVADVLCEFLEVAVHLILYVREVYPVGIFQKRKKYNVPVQMSCHPELNQYIQ
DTLHCVKPLLEKNDVEKVVVVILDKEHRPVEKFVFEITQPPLLSISSDSLLSHVEQLLRA
FILKISVCDAVLDHNPPGCTFTVLVHTREAATRNMEKIQVIKDFPWILADEQDVHMHDPR
LIPLKTMTSDILKMQLYVEERAHK

Primary citation

Insights into the scaffold mechanism of human Rev1 in translesional synthesis revealed by structural studies on its polymerase-interacting domain. Liu, D.N., Ryu, K.S., Ko, J.S. et al. To be published.

Other PDB entries of the same protein (UniProt Q9UBZ9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6WS0 2.24 Å, Rational drug design of phenazopyridine derivatives as novel inhibitors of Rev1-CT
6ASR 2.36 Å, REV1 UBM2 domain complex with ubiquitin
6WS5 2.47 Å, Rational drug design of phenazopyridine derivatives as novel inhibitors of Rev1-CT
3GQC 2.5 Å, Structure of human Rev1-DNA-dNTP ternary complex
4GK0 2.7 Å, Crystal structure of human Rev3-Rev7-Rev1 complex
9VGW 2.7 Å, Crystal structure of human PCNA in complex with REV1 PIP-box
4BA9 2.73 Å, The structural basis for the coordination of Y-family Translesion DNA Polymerases by Rev1
3VU7 2.8 Å, Crystal structure of REV1-REV7-REV3 ternary complex
4GK5 3.21 Å, Crystal structure of human Rev3-Rev7-Rev1-Polkappa complex
2EBW Solution structure of the BRCT domain from human DNA repair protein REV1
2LSI Solution structure of polymerase-interacting domain of human Rev1 in complex with…
2LSK C-terminal domain of human REV1 in complex with DNA-polymerase H (eta)

Browse structure collections

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