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1IBU

STRUCTURE OF THE D53,54N MUTANT OF HISTIDINE DECARBOXYLASE AT 25 C

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 SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: Proton donor
ChainResidueDetails
BGLU197
DGLU197
FGLU197

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING:
ChainResidueDetails
BPYR82
DPYR82
FPYR82

site_idSWS_FT_FI3
Number of Residues3
DetailsSITE: Cleavage (non-hydrolytic)
ChainResidueDetails
BPYR82
DPYR82
FPYR82

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: Pyruvic acid (Ser) => ECO:0000269|PubMed:6698997
ChainResidueDetails
BPHE83
DPHE83
FPHE83

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1pya
ChainResidueDetails
ESER81

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pya
ChainResidueDetails
ASER81
BPHE195
BGLU197

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pya
ChainResidueDetails
CSER81
DPHE195
DGLU197

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1pya
ChainResidueDetails
FPHE195
FGLU197

site_idMCSA1
Number of Residues4
DetailsM-CSA 49
ChainResidueDetails
BPYR82hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BPHE83covalently attached, electrofuge, electron pair acceptor, electron pair donor, electrophile, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
BPHE195electrostatic stabiliser, hydrogen bond donor
BGLU197hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_idMCSA2
Number of Residues4
DetailsM-CSA 49
ChainResidueDetails
DPYR82hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
DPHE83covalently attached, electrofuge, electron pair acceptor, electron pair donor, electrophile, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
DPHE195electrostatic stabiliser, hydrogen bond donor
DGLU197hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

site_idMCSA3
Number of Residues4
DetailsM-CSA 49
ChainResidueDetails
FPYR82hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
FPHE83covalently attached, electrofuge, electron pair acceptor, electron pair donor, electrophile, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay
FPHE195electrostatic stabiliser, hydrogen bond donor
FGLU197hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2024-07-24

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