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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

8VM5

Composite structure of human FASN with NADPH in State 5

Functional Information from GO Data
ChainGOidnamespacecontents
A0001649biological_processosteoblast differentiation
A0003723molecular_functionRNA binding
A0004312molecular_functionfatty acid synthase activity
A0004313molecular_function[acyl-carrier-protein] S-acetyltransferase activity
A0004314molecular_function[acyl-carrier-protein] S-malonyltransferase activity
A0004315molecular_function3-oxoacyl-[acyl-carrier-protein] synthase activity
A0004316molecular_function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006084biological_processacetyl-CoA metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0007584biological_processresponse to nutrient
A0008610biological_processlipid biosynthetic process
A0009058biological_processbiosynthetic process
A0016020cellular_componentmembrane
A0016297molecular_functionfatty acyl-[ACP] hydrolase activity
A0016491molecular_functionoxidoreductase activity
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0019171molecular_function(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity
A0031177molecular_functionphosphopantetheine binding
A0031667biological_processresponse to nutrient levels
A0042470cellular_componentmelanosome
A0042802molecular_functionidentical protein binding
A0044788biological_processhost-mediated perturbation of viral process
A0045296molecular_functioncadherin binding
A0046949biological_processfatty-acyl-CoA biosynthetic process
A0070062cellular_componentextracellular exosome
A0141148molecular_functionenoyl-[acyl-carrier-protein] reductase (NADPH) activity
B0001649biological_processosteoblast differentiation
B0003723molecular_functionRNA binding
B0004312molecular_functionfatty acid synthase activity
B0004313molecular_function[acyl-carrier-protein] S-acetyltransferase activity
B0004314molecular_function[acyl-carrier-protein] S-malonyltransferase activity
B0004315molecular_function3-oxoacyl-[acyl-carrier-protein] synthase activity
B0004316molecular_function3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006084biological_processacetyl-CoA metabolic process
B0006631biological_processfatty acid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0007584biological_processresponse to nutrient
B0008610biological_processlipid biosynthetic process
B0009058biological_processbiosynthetic process
B0016020cellular_componentmembrane
B0016297molecular_functionfatty acyl-[ACP] hydrolase activity
B0016491molecular_functionoxidoreductase activity
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0019171molecular_function(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity
B0031177molecular_functionphosphopantetheine binding
B0031667biological_processresponse to nutrient levels
B0042470cellular_componentmelanosome
B0042802molecular_functionidentical protein binding
B0044788biological_processhost-mediated perturbation of viral process
B0045296molecular_functioncadherin binding
B0046949biological_processfatty-acyl-CoA biosynthetic process
B0070062cellular_componentextracellular exosome
B0141148molecular_functionenoyl-[acyl-carrier-protein] reductase (NADPH) activity
Functional Information from PROSITE/UniProt
site_idPS00012
Number of Residues16
DetailsPHOSPHOPANTETHEINE Phosphopantetheine attachment site. DLGLDSLMSVEVRQTL
ChainResidueDetails
AASP2151-LEU2166
site_idPS00606
Number of Residues17
DetailsKS3_1 Ketosynthase family 3 (KS3) active site signature. GPSiaLDtACSSSlmAL
ChainResidueDetails
AGLY152-LEU168
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues776
DetailsRegion: {"description":"Acyl and malonyl transferases","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues254
DetailsRegion: {"description":"C-terminal hotdog fold","evidences":[{"source":"PROSITE-ProRule","id":"PRU01363","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues456
DetailsRegion: {"description":"Enoyl reductase","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues6
DetailsActive site: {"description":"For beta-ketoacyl synthase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01348","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsActive site: {"description":"For malonyltransferase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU10022","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues2
DetailsActive site: {"description":"Proton acceptor; for dehydratase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01363","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsActive site: {"description":"Proton donor; for dehydratase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01363","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P19096","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues64
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues16
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P19096","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P19096","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues4
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"26851298","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

251174

PDB entries from 2026-03-25

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