Research workbench
Impact of BRCA1 brct domain missense substitutions on phospho-peptide recognition: R1699Q
Analyse Impact of BRCA1 brct domain missense substitutions on phospho-peptide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PXC
- Type
- protein
- Length
- 206 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Breast cancer type 1 susceptibility protein
- EC
- 6.3.2.-
- UniProt
- P38398
- Ligands
- NI, SO4
Structure
x-ray diffraction · 1 distinct chain · 35% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Breast cancer type 1 susceptibility protein (EC 6.3.2.-) | protein | 206 | 35% helix, 19% strand | P38398 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3PXC · Impact of BRCA1 BRCT domain missense substitutions on phospho-peptide recognition: R1699Q · the same entry in another collection · chain X against X, 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 X 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 3PXC · PDBe 3PXC · UniProt P38398
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