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The structure of a CoA-dependent acyl-homoserine lactone synthase, bjai, with mta and isovaleryl-CoA

Analyse The structure of a CoA-dependent acyl-homoserine lactone synthase, bjai, with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5W8C
Type: protein
Length: 211 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Autoinducer synthase
UniProt: A0A0N0C224
Ligands: IVC, MTA, CL
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Autoinducer synthase	protein	211	35% helix, 27% strand	A0A0N0C224

Ligands and binding sites

IVC · Isovaleryl-coenzyme A · ligand · chains A
MTA · 5'-deoxy-5'-methylthioadenosine · ligand · chains A
CL · Chloride ion · ion · 2 copies · chains A
GOL · Glycerol · 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	371	0.72	0.83	37	IVC, MTA, CL

Compared structures

5W8C · The structure of a COA-dependent acyl-homoserine lactone synthase, BjaI, with MTA and… · 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 A0A0N0C224
Elsewhere: RCSB PDB 5W8C · PDBe 5W8C · UniProt A0A0N0C224

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