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3TM7

Processed Aspartate Decarboxylase Mutant with Asn72 mutated to Ala

Functional Information from GO Data
ChainGOidnamespacecontents
A0004068molecular_functionaspartate 1-decarboxylase activity
A0006523biological_processalanine biosynthetic process
B0004068molecular_functionaspartate 1-decarboxylase activity
B0006523biological_processalanine biosynthetic process
C0004068molecular_functionaspartate 1-decarboxylase activity
C0006523biological_processalanine biosynthetic process
D0004068molecular_functionaspartate 1-decarboxylase activity
D0006523biological_processalanine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE SO4 B 2
ChainResidue
BSER25
BHOH225
CHOH104
DTRP47
DARG54
BTHR57
BALA72
BALA74
BALA75
BHOH211
BHOH221
BHOH222
BHOH223

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 D 1
ChainResidue
BTRP47
BARG54
CGLY24
DSER25
DALA72
DALA74
DALA75
DHOH135

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Schiff-base intermediate with substrate; via pyruvic acid => ECO:0000269|PubMed:9546220
ChainResidueDetails
BSER25
DSER25

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
BTYR58
DTYR58

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BTHR57
BGLY73
DTHR57
DGLY73

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Pyruvic acid (Ser) => ECO:0000269|PubMed:9546220
ChainResidueDetails
BSER25
DSER25

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 409
ChainResidueDetails
BSER25covalently attached, electrofuge, electrophile
BTYR58activator, increase nucleophilicity, proton acceptor, proton donor

site_idMCSA2
Number of Residues2
DetailsM-CSA 409
ChainResidueDetails
DSER25covalently attached, electrofuge, electrophile
DTYR58activator, increase nucleophilicity, proton acceptor, proton donor

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PDB entries from 2025-06-18

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