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2CF2

Architecture of mammalian fatty acid synthase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004315molecular_function3-oxoacyl-[acyl-carrier-protein] synthase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006633biological_processfatty acid biosynthetic process
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0044281biological_processsmall molecule metabolic process
A1903966biological_processmonounsaturated fatty acid biosynthetic process
B0016740molecular_functiontransferase activity
C0005737cellular_componentcytoplasm
C0006633biological_processfatty acid biosynthetic process
C0008693molecular_function(3R)-3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity
D0016491molecular_functionoxidoreductase activity
J0004315molecular_function3-oxoacyl-[acyl-carrier-protein] synthase activity
J0005737cellular_componentcytoplasm
J0005829cellular_componentcytosol
J0006633biological_processfatty acid biosynthetic process
J0016746molecular_functionacyltransferase activity
J0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
J0044281biological_processsmall molecule metabolic process
J1903966biological_processmonounsaturated fatty acid biosynthetic process
K0016740molecular_functiontransferase activity
L0005737cellular_componentcytoplasm
L0006633biological_processfatty acid biosynthetic process
L0008693molecular_function(3R)-3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity
M0016491molecular_functionoxidoreductase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348, ECO:0000305|PubMed:10571059
ChainResidueDetails
ASER163
JSER163

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348
ChainResidueDetails
AHIS298
AHIS333
JHIS298
JHIS333

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 292
ChainResidueDetails
ASER163activator, covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile
AHIS298electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ALYS328activator, hydrogen bond donor
AHIS333electrostatic stabiliser, hydrogen bond donor, increase basicity
APHE390activator, hydrogen bond acceptor
APHE392electrostatic stabiliser, hydrogen bond donor

site_idMCSA2
Number of Residues6
DetailsM-CSA 292
ChainResidueDetails
JSER163activator, covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile
JHIS298electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
JLYS328activator, hydrogen bond donor
JHIS333electrostatic stabiliser, hydrogen bond donor, increase basicity
JPHE390activator, hydrogen bond acceptor
JPHE392electrostatic stabiliser, hydrogen bond donor

site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
CVAL1076
CGLY1079
CHIS1070
CCYS1080

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
LASP1084

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
LVAL1076
LGLY1079
LHIS1070
LCYS1080

site_idCSA4
Number of Residues1
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
CASP1084

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
BSER97
BHIS201
BGLN250

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
KSER97
KHIS201
KGLN250

site_idCSA7
Number of Residues1
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
DTYR49

site_idCSA8
Number of Residues1
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
MTYR49

site_idCSA9
Number of Residues6
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
APHE392
ALYS328
AHIS298
AHIS333
APHE390
ASER163

site_idCSA10
Number of Residues6
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
JPHE392
JLYS328
JHIS298
JHIS333
JPHE390
JSER163

site_idCSA11
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ELYS155
ETYR151

site_idCSA12
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
ELYS155
EGLN148

site_idCSA13
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
NLYS155
NGLN148

site_idCSA14
Number of Residues2
DetailsAnnotated By Reference To The Literature 1eq2
ChainResidueDetails
NLYS155
NTYR151

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PDB entries from 2024-05-01

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