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1PYA

REFINED STRUCTURE OF THE PYRUVOYL-DEPENDENT HISTIDINE DECARBOXYLASE FROM LACTOBACILLUS 30A

Functional Information from GO Data
ChainGOidnamespacecontents
A0004398molecular_functionhistidine decarboxylase activity
A0006520biological_processamino acid metabolic process
A0006547biological_processL-histidine metabolic process
A0016831molecular_functioncarboxy-lyase activity
B0004398molecular_functionhistidine decarboxylase activity
B0006520biological_processamino acid metabolic process
B0006547biological_processL-histidine metabolic process
B0016831molecular_functioncarboxy-lyase activity
C0004398molecular_functionhistidine decarboxylase activity
C0006520biological_processamino acid metabolic process
C0006547biological_processL-histidine metabolic process
C0016831molecular_functioncarboxy-lyase activity
D0004398molecular_functionhistidine decarboxylase activity
D0006520biological_processamino acid metabolic process
D0006547biological_processL-histidine metabolic process
D0016831molecular_functioncarboxy-lyase activity
E0004398molecular_functionhistidine decarboxylase activity
E0006520biological_processamino acid metabolic process
E0006547biological_processL-histidine metabolic process
E0016831molecular_functioncarboxy-lyase activity
F0004398molecular_functionhistidine decarboxylase activity
F0006520biological_processamino acid metabolic process
F0006547biological_processL-histidine metabolic process
F0016831molecular_functioncarboxy-lyase activity
Functional Information from PDB Data
site_idACB
Number of Residues1
DetailsACTIVE SITE 1
ChainResidue
BPYR82

site_idACD
Number of Residues1
DetailsACTIVE SITE 2
ChainResidue
DPYR82

site_idACF
Number of Residues1
DetailsACTIVE SITE 3
ChainResidue
FPYR82

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Proton donor"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 2745463
ChainResidueDetails
ATYR62
FPHE195
FGLU197
ESER81

site_idCSA2
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 2745463
ChainResidueDetails
ASER81
CTYR62
BPHE195
BGLU197

site_idCSA3
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 2745463
ChainResidueDetails
CSER81
DPHE195
DGLU197
ETYR62

site_idMCSA1
Number of Residues2
DetailsM-CSA 49
ChainResidueDetails
BALA199electrostatic stabiliser, hydrogen bond donor
BVAL201hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AGLU66activator, hydrogen bond acceptor
ASER81hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_idMCSA2
Number of Residues2
DetailsM-CSA 49
ChainResidueDetails
DALA199electrostatic stabiliser, hydrogen bond donor
DVAL201hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
CGLU66activator, hydrogen bond acceptor
CSER81hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_idMCSA3
Number of Residues2
DetailsM-CSA 49
ChainResidueDetails
FALA199electrostatic stabiliser, hydrogen bond donor
FVAL201hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
EGLU66activator, hydrogen bond acceptor
ESER81hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2025-07-30

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