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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
DetailsActive site: {"description":"Proton donor"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues1
DetailsM-CSA 409
ChainResidueDetails
BALA62activator, increase nucleophilicity, proton acceptor, proton donor

242842

PDB entries from 2025-10-08

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