2CF2
Architecture of mammalian fatty acid synthase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004315 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] synthase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0006633 | biological_process | fatty acid biosynthetic process |
A | 0016746 | molecular_function | acyltransferase activity |
A | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
A | 0044281 | biological_process | small molecule metabolic process |
A | 1903966 | biological_process | monounsaturated fatty acid biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0006633 | biological_process | fatty acid biosynthetic process |
C | 0008693 | molecular_function | (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity |
D | 0016491 | molecular_function | oxidoreductase activity |
J | 0004315 | molecular_function | 3-oxoacyl-[acyl-carrier-protein] synthase activity |
J | 0005737 | cellular_component | cytoplasm |
J | 0005829 | cellular_component | cytosol |
J | 0006633 | biological_process | fatty acid biosynthetic process |
J | 0016746 | molecular_function | acyltransferase activity |
J | 0016747 | molecular_function | acyltransferase activity, transferring groups other than amino-acyl groups |
J | 0044281 | biological_process | small molecule metabolic process |
J | 1903966 | biological_process | monounsaturated fatty acid biosynthetic process |
K | 0016740 | molecular_function | transferase activity |
L | 0005737 | cellular_component | cytoplasm |
L | 0006633 | biological_process | fatty acid biosynthetic process |
L | 0008693 | molecular_function | (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity |
M | 0016491 | molecular_function | oxidoreductase activity |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348, ECO:0000305|PubMed:10571059 |
Chain | Residue | Details |
A | SER163 | |
J | SER163 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348 |
Chain | Residue | Details |
A | HIS298 | |
A | HIS333 | |
J | HIS298 | |
J | HIS333 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 292 |
Chain | Residue | Details |
A | SER163 | activator, covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile |
A | HIS298 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | LYS328 | activator, hydrogen bond donor |
A | HIS333 | electrostatic stabiliser, hydrogen bond donor, increase basicity |
A | PHE390 | activator, hydrogen bond acceptor |
A | PHE392 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 292 |
Chain | Residue | Details |
J | SER163 | activator, covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile |
J | HIS298 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
J | LYS328 | activator, hydrogen bond donor |
J | HIS333 | electrostatic stabiliser, hydrogen bond donor, increase basicity |
J | PHE390 | activator, hydrogen bond acceptor |
J | PHE392 | electrostatic stabiliser, hydrogen bond donor |
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
C | VAL1076 | |
C | GLY1079 | |
C | HIS1070 | |
C | CYS1080 |
site_id | CSA2 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
L | ASP1084 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
L | VAL1076 | |
L | GLY1079 | |
L | HIS1070 | |
L | CYS1080 |
site_id | CSA4 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
C | ASP1084 |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
B | SER97 | |
B | HIS201 | |
B | GLN250 |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
K | SER97 | |
K | HIS201 | |
K | GLN250 |
site_id | CSA7 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
D | TYR49 |
site_id | CSA8 |
Number of Residues | 1 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
M | TYR49 |
site_id | CSA9 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
A | PHE392 | |
A | LYS328 | |
A | HIS298 | |
A | HIS333 | |
A | PHE390 | |
A | SER163 |
site_id | CSA10 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
J | PHE392 | |
J | LYS328 | |
J | HIS298 | |
J | HIS333 | |
J | PHE390 | |
J | SER163 |
site_id | CSA11 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
E | LYS155 | |
E | TYR151 |
site_id | CSA12 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
E | LYS155 | |
E | GLN148 |
site_id | CSA13 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
N | LYS155 | |
N | GLN148 |
site_id | CSA14 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1eq2 |
Chain | Residue | Details |
N | LYS155 | |
N | TYR151 |