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Crystal structure of the BRCA1 brct domains in complex with the phosphorylated interacting region from BACH1 helicase

Analyse Crystal structure of the BRCA1 brct domains in complex with the phosphorylated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1T15
Type: protein
Length: 219 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Breast cancer type 1 susceptibility protein; BRCA1 interacting protein C-terminal…
UniProt: P38398
Pockets: 1 · best druggability 0.27

Structure

x-ray diffraction · 2 distinct chains · 33% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Breast cancer type 1 susceptibility protein	protein	211	35% helix, 18% strand	P38398
B	BRCA1 interacting protein C-terminal helicase 1	protein	8	0% helix, 13% strand	—

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	54	0.27	0.74	14	empty

Interfaces

1 interface between chains.

A–B · 524 Å² buried · 9 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

1T15 · Crystal Structure of the Brca1 BRCT Domains in Complex with the Phosphorylated… · the same entry in another collection · chain A against A, TM-score 1.00
P38398 · AlphaFold monomer V2.0 prediction for breast cancer type 1 susceptibility protein (P38398) · a predicted model of the same protein · chain A 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 P38398
Elsewhere: RCSB PDB 1T15 · PDBe 1T15 · UniProt P38398

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