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Crystal structure of the brct domain of S. cerevisiae REV1

Analyse Crystal structure of the brct domain of S. cerevisiae REV1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4ID3
Type: protein
Length: 174 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA repair protein REV1
EC: 2.7.7.-
UniProt: P12689
Pockets: 1 · best druggability 0.35

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	DNA repair protein REV1 (EC 2.7.7.-)	protein	87	33% helix, 15% strand	P12689

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	89	0.35	0.75	14	empty

Interfaces

1 interface between chains.

A–B · 429 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

4ID3 · Crystal Structure of the BRCT domain of S. Cerevisiae Rev1 · the same entry in another collection · chain A against A, TM-score 1.00
P12689 · AlphaFold monomer V2.0 prediction for DNA repair protein REV1 (P12689) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P12689
Elsewhere: RCSB PDB 4ID3 · PDBe 4ID3 · UniProt P12689

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