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2QQD

N47A mutant of Pyruvoyl-dependent Arginine Decarboxylase from Methanococcus jannashii

Functional Information from GO Data
ChainGOidnamespacecontents
A0006520biological_processamino acid metabolic process
A0006527biological_processarginine catabolic process
A0008792molecular_functionarginine decarboxylase activity
A0016831molecular_functioncarboxy-lyase activity
B0006520biological_processamino acid metabolic process
B0006527biological_processarginine catabolic process
B0008792molecular_functionarginine decarboxylase activity
B0016831molecular_functioncarboxy-lyase activity
C0006520biological_processamino acid metabolic process
C0006527biological_processarginine catabolic process
C0008792molecular_functionarginine decarboxylase activity
C0016831molecular_functioncarboxy-lyase activity
D0006520biological_processamino acid metabolic process
D0006527biological_processarginine catabolic process
D0008792molecular_functionarginine decarboxylase activity
D0016831molecular_functioncarboxy-lyase activity
E0006520biological_processamino acid metabolic process
E0006527biological_processarginine catabolic process
E0008792molecular_functionarginine decarboxylase activity
E0016831molecular_functioncarboxy-lyase activity
F0006520biological_processamino acid metabolic process
F0006527biological_processarginine catabolic process
F0008792molecular_functionarginine decarboxylase activity
F0016831molecular_functioncarboxy-lyase activity
G0006520biological_processamino acid metabolic process
G0006527biological_processarginine catabolic process
G0008792molecular_functionarginine decarboxylase activity
G0016831molecular_functioncarboxy-lyase activity
H0006520biological_processamino acid metabolic process
H0006527biological_processarginine catabolic process
H0008792molecular_functionarginine decarboxylase activity
H0016831molecular_functioncarboxy-lyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE AG2 B 671
ChainResidue
ASER52
CLEU38
CGLY44
AHOH689
BILE54
BILE107
BMET108
BGLU109
CLEU31
CPHE34
CASP35

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE AG2 A 671
ChainResidue
ALEU31
APHE34
AASP35
ALEU38
AGLY44
DSER52
EILE54
EILE107
EGLU109
EARG134

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PYR B 53
ChainResidue
AILE51
BILE54
BLEU106
BILE107

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PYR E 53
ChainResidue
DILE51
DSER52
EILE54
ELEU106
EILE107

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MPD C 700
ChainResidue
AHOH689
CLEU31
CPHE34
CTYR79

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MPD D 700
ChainResidue
ALEU31
APHE34
BTYR79
DARG50
DSER52
DHOH732

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsSITE: Cleavage (non-hydrolytic)
ChainResidueDetails
CSER52
FSER52
GSER52
HSER52

site_idSWS_FT_FI2
Number of Residues4
DetailsMOD_RES: Pyruvic acid (Ser) => ECO:0000269|PubMed:11980912
ChainResidueDetails
CSER53
FSER53
GSER53
HSER53

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 707
ChainResidueDetails
CALA47
CSER52
CSER53
CGLU109proton shuttle (general acid/base)

site_idMCSA2
Number of Residues4
DetailsM-CSA 707
ChainResidueDetails
FALA47
FSER52
FSER53
FGLU109proton shuttle (general acid/base)

site_idMCSA3
Number of Residues4
DetailsM-CSA 707
ChainResidueDetails
GALA47
GSER52
GSER53
GGLU109proton shuttle (general acid/base)

site_idMCSA4
Number of Residues4
DetailsM-CSA 707
ChainResidueDetails
HALA47
HSER52
HSER53
HGLU109proton shuttle (general acid/base)

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PDB entries from 2024-11-06

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