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1.3 ångström structure of N-acyl homoserine lactone hydrolase with the product N-hexanoyl-L-homocysteine bound to the catalytic metal center

Analyse 1.3 ångström structure of N-acyl homoserine lactone hydrolase with the product… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3DHC
Type: protein
Length: 250 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N-acyl homoserine lactone hydrolase
EC: 3.1.1.-
UniProt: Q7B8B9
Ligands: CYK, ZN
Pockets: 1 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 30% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N-acyl homoserine lactone hydrolase (EC 3.1.1.-)	protein	250	26% helix, 30% strand	Q7B8B9

Ligands and binding sites

CYK · N-hexanoyl-L-homocysteine · ligand · chains A
ZN · Zinc ion · metal · 2 copies · chains A
GOL · Glycerol · additive · 6 copies · 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	260	0.66	0.82	32	CYK

Compared structures

3DHC · 1.3 Angstrom Structure of N-Acyl Homoserine Lactone Hydrolase with the Product… · 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 Q7B8B9
Elsewhere: RCSB PDB 3DHC · PDBe 3DHC · UniProt Q7B8B9

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