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Crystal structure of the BARD1 brct mutant

Analyse Crystal structure of the BARD1 brct mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6M14
Type: protein
Length: 418 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: BRCA1-associated ring domain protein 1
EC: 2.3.2.27
UniProt: Q99728
Ligands: SO4
Pockets: 2 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 34% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A	BRCA1-associated ring domain protein 1 (EC 2.3.2.27)	protein	209	34% helix, 16% strand	Q99728

Ligands and binding sites

SO4 · Sulfate ion · ion · chains A

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	376	0.69	0.81	44	empty
2	311	0.64	0.80	36	empty

Interfaces

1 interface between chains.

B–A · 787 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

6M14 · Crystal Structure of the BARD1 BRCT Mutant · the same entry in another collection · chain B against B, 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 6M14 · PDBe 6M14 · UniProt Q99728

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