MolNFT v1 · #102219 · protein
Crystal structure of human BRCA1 brct in complex with nonphosphopeptide inhibitor
4OFB · Breast cancer type 1 susceptibility protein: “Crystal structure of human BRCA1 brct in complex with nonphosphopeptide inhibitor”. X-ray diffraction, 2 ligands (ACE, NH2), 2 pockets (best druggability 0.43). MolNFT v1 #102219 on…
- PDB
- 4OFB
- Type
- protein
- Length
- 221 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Breast cancer type 1 susceptibility protein; Nonphosphopeptide inhibitor
- UniProt
- P38398
- Ligands
- ACE, NH2
- Pockets
- 2 · best druggability 0.43
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 | 209 | 35% helix, 19% strand | P38398 |
| B | Nonphosphopeptide inhibitor | protein | 12 | 0% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 104 | 0.43 | 0.78 | 18 | empty |
| 2 | 62 | 0.35 | 0.78 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 736 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified, 1 covalent (nonstandard, covalent ligand).
Compared structures
- 4OFB · Crystal structure of human BRCA1 BRCT in complex with nonphosphopeptide inhibitor · 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 4OFB · PDBe 4OFB · UniProt P38398
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