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X-ray Crystal Structure of L-Azetidine-2-Carboxylate Hydrolase

Analyse X-ray Crystal Structure of L-Azetidine-2-Carboxylate Hydrolase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3SMV
Type: protein
Length: 233 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.38
Source: Pseudomonas sp. A2C
Molecule: (S)-2-haloacid dehalogenase
EC: 3.8.1.2
UniProt: B2Z3V8
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · resolution 1.38 · 1 distinct chain · 53% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	(S)-2-haloacid dehalogenase (EC 3.8.1.2)	protein	233	53% helix, 13% strand	B2Z3V8

Ligands and binding sites

GOL · Glycerol · additive · 9 copies · chains A
IMD · Imidazole · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	427	0.73	0.83	44	GOL

Compared structures

3SMV · X-ray crystal structure of L-azetidine-2-carboxylate hydrolase · 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 B2Z3V8
Elsewhere: RCSB PDB 3SMV · PDBe 3SMV · UniProt B2Z3V8

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