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3PLX

The crystal structure of aspartate alpha-decarboxylase from Campylobacter jejuni subsp. jejuni NCTC 11168

Functional Information from GO Data
ChainGOidnamespacecontents
A0004068molecular_functionaspartate 1-decarboxylase activity
A0006523biological_processalanine biosynthetic process
B0004068molecular_functionaspartate 1-decarboxylase activity
B0006523biological_processalanine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ACT B 1
ChainResidue
BPYR25
BVAL47
BARG54
BTHR57
BASN71
BGLY72
BALA73
BALA74
BILE85

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE PEG B 127
ChainResidue
ATHR16
BGLU65
BGLY66
BGLU109

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Schiff-base intermediate with substrate; via pyruvic acid => ECO:0000255|HAMAP-Rule:MF_00446
ChainResidueDetails
BPYR25

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00446
ChainResidueDetails
BTYR58

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00446
ChainResidueDetails
BTHR57
BGLY72

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Pyruvic acid (Ser) => ECO:0000255|HAMAP-Rule:MF_00446
ChainResidueDetails
BPYR25

226707

PDB entries from 2024-10-30

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