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Crystal structure of beta-ketoacyl-acp synthase III (fabh) from yersinia pestis

Analyse Crystal structure of beta-ketoacyl-acp synthase III (fabh) 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: 4YLT
Type: protein
Length: 310 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 3-oxoacyl-[acyl-carrier-protein] synthase 3
EC: 2.3.1.180
UniProt: Q8ZFT7
Pockets: 3 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 42% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	3-oxoacyl-[acyl-carrier-protein] synthase 3 (EC 2.3.1.180)	protein	310	42% helix, 27% strand	Q8ZFT7

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	192	0.65	0.84	28	empty
2	80	0.48	0.82	14	empty
3	57	0.29	0.75	12	empty

Compared structures

4YLT · Crystal structure of beta-ketoacyl-ACP synthase III (FabH) from Yersinia pestis · the same entry in another collection · chain A against A, TM-score 1.00
Q8ZFT7 · 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 Q8ZFT7
Elsewhere: RCSB PDB 4YLT · PDBe 4YLT · UniProt Q8ZFT7

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