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9NJU

Structure of native homodimer of D. discoideum polyketide synthase Pks16

Functional Information from GO Data
ChainGOidnamespacecontents
A0004312molecular_functionfatty acid synthase activity
A0004315molecular_function3-oxoacyl-[acyl-carrier-protein] synthase activity
A0005575cellular_componentcellular_component
A0006629biological_processlipid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0007618biological_processmating
A0016491molecular_functionoxidoreductase activity
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0032787biological_processmonocarboxylic acid metabolic process
A0044283biological_processsmall molecule biosynthetic process
B0004312molecular_functionfatty acid synthase activity
B0004315molecular_function3-oxoacyl-[acyl-carrier-protein] synthase activity
B0005575cellular_componentcellular_component
B0006629biological_processlipid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0007618biological_processmating
B0016491molecular_functionoxidoreductase activity
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0032787biological_processmonocarboxylic acid metabolic process
B0044283biological_processsmall molecule biosynthetic process
Functional Information from PROSITE/UniProt
site_idPS00606
Number of Residues17
DetailsKS3_1 Ketosynthase family 3 (KS3) active site signature. GPSmtLDtACSSSlnAV
ChainResidueDetails
AGLY170-VAL186

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues844
DetailsDomain: {"description":"Ketosynthase family 3 (KS3)","evidences":[{"source":"PROSITE-ProRule","id":"PRU01348","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues558
DetailsDomain: {"description":"PKS/mFAS DH","evidences":[{"source":"PROSITE-ProRule","id":"PRU01363","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues66
DetailsRegion: {"description":"Acyl/malonyl transferases"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues240
DetailsRegion: {"description":"N-terminal hotdog fold","evidences":[{"source":"PROSITE-ProRule","id":"PRU01363","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues288
DetailsRegion: {"description":"C-terminal hotdog fold","evidences":[{"source":"PROSITE-ProRule","id":"PRU01363","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsActive site: {"description":"For beta-ketoacyl synthase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01348","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsActive site: {"description":"For acyl/malonyl transferase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU10022","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsActive site: {"description":"Proton acceptor; for dehydratase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01363","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsActive site: {"description":"Proton donor; for dehydratase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01363","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

248942

PDB entries from 2026-02-11

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