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4D7Z

E. coli L-aspartate-alpha-decarboxylase mutant N72Q to a resolution of 1.9 Angstroms

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 Residues13
DetailsBINDING SITE FOR RESIDUE PEG B 1121
ChainResidue
AALA18
BHOH2037
BHOH2038
BHOH2039
BHOH2060
AHOH2030
BALA76
BHIS77
BALA79
BSER80
BSER80
BSCN1123
BHOH2037

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SCN B 1122
ChainResidue
BPYR25
BTRP47
BARG54
BALA74
BALA75
BILE86

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SCN B 1123
ChainResidue
ALEU20
BHIS77
BASP83
BPEG1121
BHOH2038
BHOH2039
BHOH2061

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Schiff-base intermediate with substrate; via pyruvic acid => ECO:0000269|PubMed:9546220
ChainResidueDetails
BPYR25

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
BTYR58

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BTHR57
BGLY73

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Pyruvic acid (Ser) => ECO:0000269|PubMed:9546220
ChainResidueDetails
BPYR25

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 409
ChainResidueDetails
BPYR25covalently attached, electrofuge, electrophile
BTYR58activator, increase nucleophilicity, proton acceptor, proton donor

222624

PDB entries from 2024-07-17

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