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Structure of C-terminal domain of human polymerase REV1 in complex with POLD3 rir-motif

Analyse Structure of C-terminal domain of human polymerase REV1 in complex with POLD3… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2N1G
Type: protein
Length: 110 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA repair protein REV1; DNA polymerase delta subunit 3
EC: 2.7.7.-
UniProt: Q9UBZ9, Q15054

Structure

solution nmr · 2 distinct chains · 61% helix, 2% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA repair protein REV1 (EC 2.7.7.-)	protein	94	71% helix, 2% strand	Q9UBZ9
B	DNA polymerase delta subunit 3	protein	16	0% helix, 0% strand	Q15054

Interfaces

1 interface between chains.

A–B · 553 Å² buried · 7 hydrogen bonds · protein-protein

Compared structures

2N1G · Structure of C-terminal domain of human polymerase Rev1 in complex with PolD3 RIR-motif · the same entry in another collection · chain A against A, TM-score 1.00
Q9UBZ9 · AlphaFold monomer V2.0 prediction for DNA repair protein REV1 (Q9UBZ9) · a predicted model of the same protein · chain A against A, TM-score 0.90
Q15054 · AlphaFold monomer V2.0 prediction for DNA polymerase delta subunit 3 (Q15054) · a predicted model of the same protein · chain B against A, TM-score 0.24

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q9UBZ9
Every structure of UniProt Q15054
Elsewhere: RCSB PDB 2N1G · PDBe 2N1G · UniProt Q9UBZ9 · UniProt Q15054

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