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An ultral high resolution structure of N-acyl homoserine lactone hydrolase with the product N-hexanoyl-L-homoserine bound at an alternative site

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

PDB: 3DHA
Type: protein
Length: 254 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: C6L, ZN
Pockets: 2 · best druggability 0.65

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	254	26% helix, 30% strand	Q7B8B9

Ligands and binding sites

C6L · N-hexanoyl-L-homoserine · ligand · chains A
ZN · Zinc ion · metal · 2 copies · chains A
GOL · Glycerol · additive · 4 copies · 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	302	0.65	0.81	32	C6L
2	51	0.27	0.75	16	GOL

Compared structures

3DHA · An Ultral High Resolution Structure of N-Acyl Homoserine Lactone Hydrolase with the… · 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 3DHA · PDBe 3DHA · UniProt Q7B8B9

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