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2VAQ

STRUCTURE OF STRICTOSIDINE SYNTHASE IN COMPLEX WITH INHIBITOR

Functional Information from GO Data
ChainGOidnamespacecontents
A0005773cellular_componentvacuole
A0009058biological_processbiosynthetic process
A0009820biological_processalkaloid metabolic process
A0012505cellular_componentendomembrane system
A0016787molecular_functionhydrolase activity
A0016829molecular_functionlyase activity
A0016844molecular_functionstrictosidine synthase activity
B0005773cellular_componentvacuole
B0009058biological_processbiosynthetic process
B0009820biological_processalkaloid metabolic process
B0012505cellular_componentendomembrane system
B0016787molecular_functionhydrolase activity
B0016829molecular_functionlyase activity
B0016844molecular_functionstrictosidine synthase activity
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE VAW A1334
ChainResidue
ATRP149
AGLU309
ALEU323
APHE324
AHOH2010
ATYR151
AVAL176
AVAL208
APHE226
AMET276
AHIS277
AGLU306
AHIS307

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE VAW B1334
ChainResidue
BTYR151
BPHE226
BMET276
BHIS277
BGLY305
BGLU306
BHIS307
BGLU309
BLEU323
BPHE324

Functional Information from PROSITE/UniProt
site_idPS00284
Number of Residues11
DetailsSERPIN Serpins signature. VSADSSFVLvA
ChainResidueDetails
AVAL214-ALA224

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN91
BASN91

Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 360
ChainResidueDetails
AGLU309activator, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity, proton acceptor, proton donor

site_idMCSA2
Number of Residues1
DetailsM-CSA 360
ChainResidueDetails
BGLU309activator, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity, proton acceptor, proton donor

221716

PDB entries from 2024-06-26

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