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Crystal structure of the BARD1 ankyrin repeat domain and its functional consequences

Analyse Crystal structure of the BARD1 ankyrin repeat domain and its functional… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3C5R
Type: protein
Length: 249 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: BRCA1-associated ring domain protein 1
UniProt: Q99728
Pockets: 1 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	BRCA1-associated ring domain protein 1	protein	125	50% helix, 0% strand	Q99728
B	BRCA1-associated ring domain protein 1	protein	124	52% helix, 0% strand	Q99728

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	409	0.57	0.74	51	empty

Interfaces

1 interface between chains.

A–B · 173 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

3C5R · Crystal Structure of the BARD1 Ankyrin Repeat Domain and Its Functional Consequences · the same entry in another collection · chain A against A, TM-score 1.00
Q99728 · AlphaFold monomer V2.0 prediction for BRCA1-associated ring domain protein 1 (Q99728) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 Q99728
Elsewhere: RCSB PDB 3C5R · PDBe 3C5R · UniProt Q99728

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