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The structure of the bifunctional ACETYLTRANSFERASE/DECARBOXYLASE lnmk from the leinamycin biosynthetic pathway revealing novel activity for a double hot dog fold

Analyse The structure of the bifunctional ACETYLTRANSFERASE/DECARBOXYLASE lnmk from the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4HZO
Type: protein
Length: 301 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Bifunctional methylmalonyl-COA:ACP ACYLTRANSFERASE/DECARBOXYLASE
UniProt: Q8GGP1
Ligands: COA, CL
Pockets: 3 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 37% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Bifunctional methylmalonyl-COA:ACP ACYLTRANSFERASE/DECARBOXYLASE	protein	301	22% helix, 37% strand	Q8GGP1

Ligands and binding sites

COA · Coenzyme A · ligand · chains A
CL · Chloride ion · ion · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	169	0.68	0.87	26	empty
2	255	0.64	0.82	39	CL, COA
3	62	0.26	0.73	16	empty

Compared structures

4HZO · The Structure of the Bifunctional Acetyltransferase/Decarboxylase LnmK from 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 Q8GGP1
Elsewhere: RCSB PDB 4HZO · PDBe 4HZO · UniProt Q8GGP1

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