Research workbench

Leishmania infantum BRC1 repeat in complex with LIRAD51

Analyse Leishmania infantum BRC1 repeat in complex with LIRAD51 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7QV8
Type: protein
Length: 231 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: DNA repair protein RAD51 homolog; DNA_REPAIR_PROTEIN_BRCA2_-_putative
UniProt: A4I3C9, A4HYJ9
Ligands: ADP, MG
Pockets: 1 · best druggability 0.32

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	DNA repair protein RAD51 homolog	protein	208	35% helix, 29% strand	A4I3C9
D	DNA_REPAIR_PROTEIN_BRCA2_-_putative	protein	23	17% helix, 57% strand	A4HYJ9

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

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	51	0.32	0.78	16	ADP

Interfaces

1 interface between chains.

A–D · 644 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

7QV8 · Leishmania infantum BRC1 repeat in complex with LiRAD51 · the same entry in another collection · chain A against A, TM-score 1.00

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 A4I3C9
Every structure of UniProt A4HYJ9
Elsewhere: RCSB PDB 7QV8 · PDBe 7QV8 · UniProt A4I3C9 · UniProt A4HYJ9

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