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Crystal structure of beta-ketoacyl-acp synthase III + malonyl-CoA

Analyse Crystal structure of beta-ketoacyl-acp synthase III + malonyl-CoA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1HNJ
Type: protein
Length: 317 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-ketoacyl-acyl carrier protein synthase III
EC: 2.3.1.41
UniProt: P0A6R0
Ligands: MLC, PO4
Pockets: 1 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-ketoacyl-acyl carrier protein synthase III (EC 2.3.1.41)	protein	317	40% helix, 25% strand	P0A6R0

Ligands and binding sites

MLC · Malonyl-coenzyme A · ligand · chains A
PO4 · Phosphate ion · ion · 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	251	0.69	0.85	44	MLC

Compared structures

1HNJ · Crystal structure of beta-ketoacyl-acp synthase III + malonyl-CoA · the same entry in another collection · chain A against A, TM-score 1.00
P0A6R0 · AlphaFold monomer V2.0 prediction for 3-oxoacyl-[acyl-carrier- protein] synthase 3… · a predicted model of the same protein · 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 P0A6R0
Elsewhere: RCSB PDB 1HNJ · PDBe 1HNJ · UniProt P0A6R0

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