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Human fatty acid synthase: structure and substrate selectivity of the thioesterase domain

Analyse Human fatty acid synthase: structure and substrate selectivity of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1XKT
Type: protein
Length: 520 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fatty acid synthase
UniProt: P49327
Pockets: 4 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Fatty acid synthase	protein	260	43% helix, 13% strand	P49327

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	742	0.78	0.82	53	empty
2	182	0.51	0.77	31	empty
3	214	0.51	0.76	25	empty
4	162	0.48	0.77	24	empty

Interfaces

1 interface between chains.

A–B · 627 Å² buried · 9 hydrogen bonds · protein-protein

Compared structures

1XKT · Human fatty acid synthase: Structure and substrate selectivity of the thioesterase domain · the same entry in another collection · chain A against A, TM-score 1.00
P49327 · AlphaFold monomer V2.0 prediction for fatty acid synthase (P49327) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P49327
Elsewhere: RCSB PDB 1XKT · PDBe 1XKT · UniProt P49327

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