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9D30

Cryo-EM structure of mycocerosic acid synthase with a single DH-ACP crosslink using C16 alpha-bromoamide. Complex C

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004312molecular_functionfatty acid synthase activity
A0005737cellular_componentcytoplasm
A0005886cellular_componentplasma membrane
A0006629biological_processlipid metabolic process
A0006631biological_processfatty acid metabolic process
A0006633biological_processfatty acid biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016740molecular_functiontransferase activity
A0016787molecular_functionhydrolase activity
A0016874molecular_functionligase activity
A0050111molecular_functionmycocerosate synthase activity
A0071770biological_processDIM/DIP cell wall layer assembly
B0003824molecular_functioncatalytic activity
B0004312molecular_functionfatty acid synthase activity
B0005737cellular_componentcytoplasm
B0005886cellular_componentplasma membrane
B0006629biological_processlipid metabolic process
B0006631biological_processfatty acid metabolic process
B0006633biological_processfatty acid biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016740molecular_functiontransferase activity
B0016787molecular_functionhydrolase activity
B0016874molecular_functionligase activity
B0050111molecular_functionmycocerosate synthase activity
B0071770biological_processDIM/DIP cell wall layer assembly
Functional Information from PROSITE/UniProt
site_idPS00012
Number of Residues16
DetailsPHOSPHOPANTETHEINE Phosphopantetheine attachment site. EYGLDSLGMLEMRTHV
ChainResidueDetails
AGLU2055-VAL2070

site_idPS00606
Number of Residues17
DetailsKS3_1 Ketosynthase family 3 (KS3) active site signature. GPAmtFDtACSSGlmAV
ChainResidueDetails
AGLY168-VAL184

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues570
DetailsDomain: {"description":"PKS/mFAS DH","evidences":[{"source":"PROSITE-ProRule","id":"PRU01363","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues75
DetailsDomain: {"description":"Carrier","evidences":[{"source":"PROSITE-ProRule","id":"PRU00258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues240
DetailsRegion: {"description":"N-terminal hotdog fold","evidences":[{"source":"PROSITE-ProRule","id":"PRU01363","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues300
DetailsRegion: {"description":"C-terminal hotdog fold","evidences":[{"source":"PROSITE-ProRule","id":"PRU01363","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsActive site: {"description":"Proton acceptor; for dehydratase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01363","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsActive site: {"description":"Proton donor; for dehydratase activity","evidences":[{"source":"PROSITE-ProRule","id":"PRU01363","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues64
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"O-(pantetheine 4'-phosphoryl)serine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

249524

PDB entries from 2026-02-18

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