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3O24

Crystal structure of the brevianamide F prenyltransferase FtmPT1 from Aspergillus fumigatus

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0004659molecular_functionprenyltransferase activity
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0009820biological_processalkaloid metabolic process
A0009821biological_processalkaloid biosynthetic process
A0016740molecular_functiontransferase activity
A0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
A0016787molecular_functionhydrolase activity
A1902181biological_processverruculogen biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 475
ChainResidue
AARG113
ALYS294
AGLN380
ATYR382
AHOH506

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MES A 476
ChainResidue
AHIS67
ALEU27
AGLY29
AARG66
AARG66

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 478
ChainResidue
AVAL55

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21105662","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsSite: {"description":"Required for regioselectivity","evidences":[{"source":"PubMed","id":"21105662","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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