Research workbench
Crystal structure of the human carboxypeptidase A1 in complex with the phosphinic inhibitor acetyl-leu-phe-Y( PO2CH2)-phe-oh
Analyse Crystal structure of the human carboxypeptidase A1 in complex with the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4UEZ
- Type
- protein
- Length
- 613 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Human carboxypeptidase A1
- EC
- 3.4.17.1
- UniProt
- P15085
- Ligands
- LFF, ZN
- Pockets
- 1 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Human carboxypeptidase A1 (EC 3.4.17.1) | protein | 306 | 37% helix, 18% strand | P15085 |
| B | Human carboxypeptidase A1 (EC 3.4.17.1) | protein | 307 | 40% helix, 18% strand | P15085 |
Ligands and binding sites
- LFF · (2S)-3-[(R)-{(1R)-1-[(N-acetyl-L-leucyl)amino]-2-phenylethyl}(hydroxy)phosphoryl]-2-benzylpropanoic acid · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1171 | 0.80 | 0.81 | 110 | LFF |
Interfaces
1 interface between chains.
- A–B · 641 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4UEZ · Crystal structure of the human CARBOXYPEPTIDASE A1 in complex with the PHOSPHINIC… · 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 B against A, TM-score 1.00
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 4UEZ · PDBe 4UEZ · UniProt P15085
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