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Crystal Structure of the Carboxypeptidase A from Helicoverpa Armigera

Analyse Crystal Structure of the Carboxypeptidase A from Helicoverpa Armigera in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1JQG
Type: protein
Length: 409 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.5
Source: Helicoverpa armigera
Molecule: carboxypeptidase A
EC: 3.4.17.1
UniProt: O97389
Ligands: ZN
Pockets: 3 · best druggability 0.80

Structure

x-ray diffraction · resolution 2.5 · 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.

Pocket	Volume (Å³)	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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