MolNFT v1 · #22298 · protein

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

1T15 · Breast cancer type 1 susceptibility protein: “Crystal structure of the BRCA1 brct domains in complex with the phosphorylated interacting region from BACH1…”. X-ray diffraction, 1 pocket (best druggability 0.27). MolNFT v1 #22298 on…

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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