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3O2K

Crystal Structure of Brevianamide F Prenyltransferase Complexed with Brevianamide F and Dimethylallyl S-thiolodiphosphate

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 Residues12
DetailsBINDING SITE FOR RESIDUE DST A 501
ChainResidue
AARG113
ATYR450
AQRP502
AHOH516
ALYS201
ATYR203
ALYS294
ATYR296
AMET364
AGLN380
ATYR382
ATYR446

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE QRP A 502
ChainResidue
AGLY93
AMET94
AVAL95
ALEU96
AGLU102
ATYR203
ATYR205
APHE280
ATYR435
ATYR450
ADST501
AHOH513

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MES A 475
ChainResidue
ALEU27
AGLY29
AARG66
AHIS67

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CL A 476
ChainResidue
ALYS165

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:21105662
ChainResidueDetails
AMET94
ATYR382
ATYR446
ATYR450
AGLU102
AARG113
ALYS201
ATYR203
ATYR205
ALYS294
ATYR296
AGLN380

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Required for regioselectivity => ECO:0000269|PubMed:21105662
ChainResidueDetails
AGLY115

237735

PDB entries from 2025-06-18

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