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The crystal structure of BRCA1 BRCT in complex with a minimal recognition tetrapeptide with an amidated C-terminus

Analyse The crystal structure of BRCA1 BRCT in complex with a minimal recognition… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3K0H
Type
protein
Length
215 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.7
Source
Homo sapiens; SYNTHETIC CONSTRUCT
Molecule
Breast cancer type 1 susceptibility protein; phospho peptide
UniProt
P38398
Ligands
NI, CL

Structure

x-ray diffraction · resolution 2.7 · 2 distinct chains · 33% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABreast cancer type 1 susceptibility proteinprotein21133% helix, 19% strandP38398
Bphospho peptideprotein40% helix, 25% strand—

Ligands and binding sites

  • NI · Nickel (II) ion · metal · chains A
  • CL · Chloride ion · ion · chains B

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

Interfaces

1 interface between chains.

  • A–B · 378 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (phosphorylation).

Compared structures

  • 3K0H · The crystal structure of BRCA1 brct in complex with a minimal recognition tetrapeptide… · 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

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