Research workbench

Metallo-carboxypeptidase from pseudomonas aeruginosa

Analyse Metallo-carboxypeptidase from pseudomonas aeruginosa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4A37
Type: protein
Length: 751 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Metallo-carboxypeptidase
UniProt: Q9I012
Ligands: ZN
Pockets: 6 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 29% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Metallo-carboxypeptidase	protein	375	29% helix, 23% strand	Q9I012
B	Metallo-carboxypeptidase	protein	376	29% helix, 23% strand	Q9I012

Ligands and binding sites

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

6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	426	0.57	0.74	36	empty
2	329	0.56	0.76	60	empty
3	213	0.54	0.78	36	empty
4	206	0.53	0.78	32	empty
5	113	0.38	0.75	17	empty

Interfaces

1 interface between chains.

A–B · 680 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

4A37 · Metallo-carboxypeptidase from Pseudomonas Aeruginosa · 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 Q9I012
Elsewhere: RCSB PDB 4A37 · PDBe 4A37 · UniProt Q9I012

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.