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Structure of E. COLI FABF(C163A) in complex with platensimycin

Analyse Structure of E. COLI FABF(C163A) in complex with platensimycin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3HNZ
Type: protein
Length: 411 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-oxoacyl-[acyl-carrier-protein] synthase 2
EC: 2.3.1.179
UniProt: P0AAI5
Ligands: PMN
Pockets: 3 · best druggability 0.70

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3-oxoacyl-[acyl-carrier-protein] synthase 2 (EC 2.3.1.179)	protein	411	36% helix, 22% strand	P0AAI5

Ligands and binding sites

PMN · Platensimycin · ligand · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	195	0.70	0.88	40	PMN
2	68	0.36	0.77	16	empty
3	97	0.33	0.73	19	empty

Compared structures

3HNZ · Structure of E. coli FabF(C163A) in Complex with Platensimycin · the same entry in another collection · chain A against A, TM-score 1.00
P0AAI5 · AlphaFold monomer V2.0 prediction for 3-oxoacyl-[acyl-carrier- protein] synthase 2… · 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 P0AAI5
Elsewhere: RCSB PDB 3HNZ · PDBe 3HNZ · UniProt P0AAI5

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