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8CG4

The organise full-length structure of the fungal non-reducing polyketide synthase (NR-PKS) PksA

Functional Information from GO Data
ChainGOidnamespacecontents
A0004312molecular_functionfatty acid synthase activity
A0006633biological_processfatty acid biosynthetic process
A0009058biological_processbiosynthetic process
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0031177molecular_functionphosphopantetheine binding
A0042802molecular_functionidentical protein binding
A0044550biological_processsecondary metabolite biosynthetic process
A0045122biological_processaflatoxin biosynthetic process
A0102973molecular_functionnorsolorinate anthrone synthase activity
B0004312molecular_functionfatty acid synthase activity
B0006633biological_processfatty acid biosynthetic process
B0009058biological_processbiosynthetic process
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0031177molecular_functionphosphopantetheine binding
B0042802molecular_functionidentical protein binding
B0044550biological_processsecondary metabolite biosynthetic process
B0045122biological_processaflatoxin biosynthetic process
B0102973molecular_functionnorsolorinate anthrone synthase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348
ChainResidueDetails
ACYS543
AHIS678
AHIS721
BCYS543
BHIS678
BHIS721

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: For acyl/malonyl transferase activity => ECO:0000250
ChainResidueDetails
ASER993
BSER993

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: Proton acceptor; for dehydratase activity => ECO:0000255|PROSITE-ProRule:PRU01363
ChainResidueDetails
AHIS1345
BHIS1345

site_idSWS_FT_FI4
Number of Residues2
DetailsACT_SITE: Proton donor; for dehydratase activity => ECO:0000255|PROSITE-ProRule:PRU01363
ChainResidueDetails
AASP1543
BASP1543

site_idSWS_FT_FI5
Number of Residues2
DetailsACT_SITE: For thioesterase activity => ECO:0000269|PubMed:20332208
ChainResidueDetails
ASER1937
BSER1937

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: O-(pantetheine 4'-phosphoryl)serine => ECO:0000255|PROSITE-ProRule:PRU00258, ECO:0000269|PubMed:20136099
ChainResidueDetails
ASER1746
BSER1746

223790

PDB entries from 2024-08-14

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