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Structure of an inactive lactonase from geobacillus kaustophilus with bound N-butyryl-dl-homoserine lactone

Analyse Structure of an inactive lactonase from geobacillus kaustophilus with bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3OJG
Type: protein
Length: 323 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Phosphotriesterase
EC: 3.5.-.-
UniProt: Q5KZU5
Ligands: HL4, ZN, FE
Pockets: 2 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Phosphotriesterase (EC 3.5.-.-)	protein	323	47% helix, 15% strand	Q5KZU5

Ligands and binding sites

HL4 · N-[(3S)-2-oxotetrahydrofuran-3-yl]butanamide · ligand · chains A
ZN · Zinc ion · metal · chains A
FE · Fe (III) ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	275	0.59	0.78	42	HL4
2	73	0.37	0.77	14	empty

Modifications

Observed in the structure: 1 modified (carboxylation).

Compared structures

3OJG · Structure of an inactive lactonase from Geobacillus kaustophilus with bound… · 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 Q5KZU5
Elsewhere: RCSB PDB 3OJG · PDBe 3OJG · UniProt Q5KZU5

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