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Crystal structure of beta-ketoacyl-acp synthase II (fabf) from yersinia pestis

Analyse Crystal structure of beta-ketoacyl-acp synthase II (fabf) from yersinia pestis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4R8E
Type: protein
Length: 822 residues
Chains: 2
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: Q7CJ22
Pockets: 9 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	3-oxoacyl-[acyl-carrier-protein] synthase 2 (EC 2.3.1.179)	protein	411	40% helix, 21% strand	Q7CJ22

Pockets

9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	92	0.77	0.97	34	empty
2	295	0.70	0.84	54	empty
3	329	0.69	0.83	55	empty
4	139	0.60	0.84	27	empty
5	72	0.46	0.82	17	empty

Interfaces

1 interface between chains.

A–B · 2950 Å² buried · 26 hydrogen bonds · protein-protein

Compared structures

4R8E · Crystal structure of beta-ketoacyl-ACP synthase II (FabF) from Yersinia pestis · 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 Q7CJ22
Elsewhere: RCSB PDB 4R8E · PDBe 4R8E · UniProt Q7CJ22

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