Research workbench
Crystal structure of BRCA1 brct in complex with a minimal recognition tetrapeptide with a free carboxy C-terminus.
Analyse 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
- 3K0K
- Type
- protein
- Length
- 215 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Breast cancer type 1 susceptibility protein; Phospho peptide psptf-cooh
- UniProt
- P38398
- Ligands
- NI, CL
Structure
x-ray diffraction · 2 distinct chains · 32% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Breast cancer type 1 susceptibility protein | protein | 211 | 32% helix, 18% strand | P38398 |
| B | Phospho peptide psptf-cooh | protein | 4 | 0% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 381 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 3K0K · Crystal Structure of BRCA1 BRCT in complex with a minimal recognition tetrapeptide with a… · 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 3K0K · PDBe 3K0K · UniProt P38398
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