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Thioesterase domain of human fatty acid synthase (fasn-te) binding a competitive inhibitor sbp-7635

Analyse Thioesterase domain of human fatty acid synthase (fasn-te) binding a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7MHD
Type: protein
Length: 282 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fatty acid synthase
EC: 3.1.2.14
UniProt: P49327
Ligands: ZEP
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fatty acid synthase (EC 3.1.2.14)	protein	282	45% helix, 12% strand	P49327

Ligands and binding sites

ZEP · N,N-diethyl-4-{2-[(2-fluorophenyl)methyl]-1,3-thiazol-4-yl}benzene-1-sulfonamide · ligand · 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	435	0.72	0.82	44	ZEP

Compared structures

7MHD · Thioesterase Domain of Human Fatty Acid Synthase (FASN-TE) binding a competitive… · 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 7MHD · PDBe 7MHD · UniProt P49327

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