MolNFT v1 · #11564 · protein
Crystal structure of the carboxypeptidase a from helicoverpa armigera
1JQG: “Crystal structure of the carboxypeptidase a from helicoverpa armigera”. X-ray diffraction, 1 ligand (ZN), 3 pockets (best druggability 0.80). MolNFT v1 #11564 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1JQG
- Type
- protein
- Length
- 409 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Carboxypeptidase a
- EC
- 3.4.17.1
- UniProt
- O97389
- Ligands
- ZN
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Carboxypeptidase a (EC 3.4.17.1) | protein | 409 | 37% helix, 18% strand | O97389 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 426 | 0.80 | 0.89 | 59 | ZN |
| 2 | 220 | 0.53 | 0.77 | 24 | empty |
| 3 | 84 | 0.37 | 0.76 | 22 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1JQG · Crystal Structure of the Carboxypeptidase A from Helicoverpa Armigera · the same entry in another collection · 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 O97389
- Elsewhere: RCSB PDB 1JQG · PDBe 1JQG · UniProt O97389
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