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Crystal structure of aminoacylhistidine dipeptidase from vibrio alginolyticus

Analyse Crystal structure of aminoacylhistidine dipeptidase from vibrio alginolyticus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3MRU
Type: protein
Length: 980 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aminoacyl-histidine dipeptidase
EC: 3.4.13.3
UniProt: Q2LD50
Ligands: ZN
Pockets: 8 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Aminoacyl-histidine dipeptidase (EC 3.4.13.3)	protein	490	28% helix, 28% strand	Q2LD50

Ligands and binding sites

ZN · Zinc ion · metal · 4 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	708	0.83	0.87	71	empty
2	273	0.60	0.79	36	empty
3	257	0.59	0.79	33	empty
4	115	0.42	0.76	28	empty
5	101	0.40	0.77	18	empty

Interfaces

1 interface between chains.

A–B · 1287 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

3MRU · Crystal Structure of Aminoacylhistidine Dipeptidase from Vibrio alginolyticus · 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 Q2LD50
Elsewhere: RCSB PDB 3MRU · PDBe 3MRU · UniProt Q2LD50

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