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1PQH

Serine 25 to Threonine mutation of aspartate decarboxylase

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
A0016831molecular_functioncarboxy-lyase activity
B0004068molecular_functionaspartate 1-decarboxylase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006523biological_processalanine biosynthetic process
B0015940biological_processpantothenate biosynthetic process
B0016540biological_processprotein autoprocessing
B0016831molecular_functioncarboxy-lyase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 393
ChainResidue
ALYS14
AHOH539
BPRO103
BASN104
BHOH514

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MLA A 390
ChainResidue
BHIS21
BARG102
AARG12
AVAL49
ATHR50
AHOH579

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE MLA B 391
ChainResidue
ALYS9
AARG54
AILE86
BGLY24
BTHR57
BTYR58
BALA74
BALA75
BHOH432

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE MLA A 392
ChainResidue
AGLY24
ATHR57
ATYR58
AASN72
AGLY73
AALA74
AALA75
AHOH405
BLYS9
BTRP47
BARG54
BILE86

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
ATHR25
BTHR25

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
ATHR25
BTHR25

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
ATHR25covalently attached, electrofuge, electrophile
ATYR58activator, increase nucleophilicity, proton acceptor, proton donor

site_idMCSA2
Number of Residues3
DetailsM-CSA 409
ChainResidueDetails
BLYS9electrostatic stabiliser
BTHR25covalently attached, electrofuge, electrophile
BTYR58activator, increase nucleophilicity, proton acceptor, proton donor

229380

PDB entries from 2024-12-25

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