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Crystal structure of xanthomonas campestris olea H285N with cerulenin

Analyse Crystal structure of xanthomonas campestris olea H285N with cerulenin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6B2U
Type: protein
Length: 331 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-oxoacyl-[acp] synthase III
UniProt: Q8PDX2
Ligands: CER, MN
Pockets: 1 · best druggability 0.66

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3-oxoacyl-[acp] synthase III	protein	331	47% helix, 22% strand	Q8PDX2

Ligands and binding sites

CER · (2S, 3R)-3-hydroxy-4-oxo-7,10-trans,trans-dodecadienamide · ligand · chains A
MN · Manganese (II) ion · metal · 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	350	0.66	0.80	43	CER

Compared structures

6B2U · Crystal structure of Xanthomonas campestris OleA H285N with Cerulenin · the same entry in another collection · chain A against A, TM-score 1.00
Q8PDX2 · AlphaFold monomer V2.0 prediction for acyl-COA:ACYL-CoA alkyltransferase (Q8PDX2) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q8PDX2
Elsewhere: RCSB PDB 6B2U · PDBe 6B2U · UniProt Q8PDX2

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