MolNFT v1 · #41172 · protein

Structure of the mat domain of human fas with malonyl-CoA

2JFK · Fatty acid synthase: “Structure of the mat domain of human fas with malonyl-CoA”. X-ray diffraction, 1 ligand (COA), 12 pockets (best druggability 0.59). MolNFT v1 #41172 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2JFK
Type: protein
Length: 1,620 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fatty acid synthase
EC: 2.3.1.85
UniProt: P49327
Ligands: COA
Pockets: 12 · best druggability 0.59

Structure

x-ray diffraction · 4 distinct chains · 44% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fatty acid synthase (EC 2.3.1.85)	protein	401	44% helix, 16% strand	P49327
B	Fatty acid synthase (EC 2.3.1.85)	protein	404	45% helix, 16% strand	P49327
C	Fatty acid synthase (EC 2.3.1.85)	protein	405	44% helix, 16% strand	P49327
D	Fatty acid synthase (EC 2.3.1.85)	protein	410	45% helix, 16% strand	P49327

Ligands and binding sites

COA · Coenzyme A · ligand · 4 copies · chains A, B, C, D

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

12 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	285	0.59	0.78	36	COA
2	293	0.57	0.77	40	empty
3	250	0.56	0.78	38	COA
4	236	0.54	0.77	42	empty
5	210	0.51	0.76	23	empty

Interfaces

3 interfaces between chains.

A–B · 659 Å² buried · 2 hydrogen bonds · protein-protein
C–D · 640 Å² buried · 1 hydrogen bond · protein-protein
B–C · 329 Å² buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (nonstandard).

Compared structures

2JFK · Structure of the MAT domain of human FAS with malonyl-CoA · the same entry in another collection · chain D against D, 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 0.99

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 2JFK · PDBe 2JFK · UniProt P49327

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