MolNFT v2 · #129911 · protein
Crystal structure of the human CARBOXYPEPTIDASE A1 in complex with a thiirane mechanism-based inhibitor
5OM9: “Crystal structure of the human CARBOXYPEPTIDASE A1 in complex with a thiirane mechanism-based inhibitor”. X-ray diffraction at 1.8, 2 ligands (O2S, ZN). MolNFT v2 #129911 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5OM9
- Type
- protein
- Length
- 788 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.8
- Source
- Homo sapiens
- UniProt
- P15085
- Ligands
- O2S, ZN
Structure
x-ray diffraction · resolution 1.8 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 396 | — | P15085 |
| B | — | protein | 392 | — | P15085 |
Ligands and binding sites
- O2S · (2~{R})-4-methyl-2-[(1~{S})-1-sulfanylethyl]pentanoic acid · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5OM9 · Crystal structure of the human carboxypeptidase A1 in complex with a thiirane… · the same entry in another collection · chain A against A, TM-score 1.00
- P15085 · AlphaFold monomer V2.0 prediction for carboxypeptidase A1 (P15085) · 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 P15085
- Elsewhere: RCSB PDB 5OM9 · PDBe 5OM9 · UniProt P15085
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