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1PT1

Unprocessed Pyruvoyl Dependent Aspartate Decarboxylase with Histidine 11 Mutated to Alanine

Functional Information from GO Data
ChainGOidnamespacecontents
A0004068molecular_functionaspartate 1-decarboxylase activity
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006523biological_processalanine biosynthetic process
A0015940biological_processpantothenate biosynthetic process
A0016540biological_processprotein autoprocessing
A0016829molecular_functionlyase activity
A0016831molecular_functioncarboxy-lyase activity
B0004068molecular_functionaspartate 1-decarboxylase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006523biological_processalanine biosynthetic process
B0015940biological_processpantothenate biosynthetic process
B0016540biological_processprotein autoprocessing
B0016829molecular_functionlyase activity
B0016831molecular_functioncarboxy-lyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 301
ChainResidue
AGLY24
BILE86
ATHR57
AASN72
AGLY73
AALA74
AALA75
AHOH325
BTRP47
BARG54

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 302
ChainResidue
ALYS9
AALA11
AARG12
AILE86
ATYR107
BTYR22
BGLU23
BGLY24

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 B 303
ChainResidue
ATRP47
AARG54
AILE86
BGLY24
BTHR57
BASN72
BGLY73
BALA74
BALA75
BHOH402

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 304
ChainResidue
AGLU23
ASER25
AILE60
AHOH323
AHOH338
AHOH370
BLYS9
BTYR107

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
ASER25
BSER25

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
ATYR58
BTYR58

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ATHR57
AGLY73
BTHR57
BGLY73

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Pyruvic acid (Ser) => ECO:0000269|PubMed:9546220
ChainResidueDetails
ASER25
BSER25

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1aw8
ChainResidueDetails
BLYS9

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1aw8
ChainResidueDetails
ATYR58

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aw8
ChainResidueDetails
ALYS9
BTYR58

site_idMCSA1
Number of Residues3
DetailsM-CSA 409
ChainResidueDetails
ALYS9electrostatic stabiliser
ASER25covalently attached, electrofuge, electrophile
ATYR58activator, increase nucleophilicity, proton acceptor, proton donor

site_idMCSA2
Number of Residues3
DetailsM-CSA 409
ChainResidueDetails
BLYS9electrostatic stabiliser
BSER25covalently attached, electrofuge, electrophile
BTYR58activator, increase nucleophilicity, proton acceptor, proton donor

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PDB entries from 2025-06-25

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