Research workbench
Crystal structure of the tick carboxypeptidase inhibitor in complex with bovine carboxypeptidase a
Analyse Crystal structure of the tick carboxypeptidase inhibitor in complex with bovine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ZLH
- Type
- protein
- Length
- 375 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carboxypeptidase A1; Carboxypeptidase inhibitor
- EC
- 3.4.17.1
- UniProt
- P00730
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carboxypeptidase A1 (EC 3.4.17.1) | protein | 301 | 39% helix, 17% strand | P00730 |
| B | Carboxypeptidase inhibitor | protein | 74 | 31% helix, 23% strand | — |
Ligands and binding sites
- ZN · Zinc ion · metal · 5 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 193 | 0.57 | 0.80 | 45 | empty |
| 2 | 141 | 0.48 | 0.78 | 31 | empty |
Interfaces
1 interface between chains.
- A–B · 1064 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 disulfide (disulfide).
Compared structures
- 1ZLH · Crystal structure of the tick carboxypeptidase inhibitor in complex with bovine… · the same entry in another collection · chain A against A, TM-score 1.00
- P00730 · AlphaFold monomer V2.0 prediction for carboxypeptidase A1 (P00730) · a predicted model of the same protein · chain A 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 P00730
- Elsewhere: RCSB PDB 1ZLH · PDBe 1ZLH · UniProt P00730
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