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1G2W

E177S MUTANT OF THE PYRIDOXAL-5'-PHOSPHATE ENZYME D-AMINO ACID AMINOTRANSFERASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005829cellular_componentcytosol
A0008483molecular_functiontransaminase activity
A0008652biological_processamino acid biosynthetic process
A0016740molecular_functiontransferase activity
A0019478biological_processD-amino acid catabolic process
A0019752biological_processcarboxylic acid metabolic process
A0030170molecular_functionpyridoxal phosphate binding
A0046394biological_processcarboxylic acid biosynthetic process
A0046416biological_processD-amino acid metabolic process
A0046437biological_processD-amino acid biosynthetic process
A0047810molecular_functionD-alanine-2-oxoglutarate aminotransferase activity
B0003824molecular_functioncatalytic activity
B0005829cellular_componentcytosol
B0008483molecular_functiontransaminase activity
B0008652biological_processamino acid biosynthetic process
B0016740molecular_functiontransferase activity
B0019478biological_processD-amino acid catabolic process
B0019752biological_processcarboxylic acid metabolic process
B0030170molecular_functionpyridoxal phosphate binding
B0046394biological_processcarboxylic acid biosynthetic process
B0046416biological_processD-amino acid metabolic process
B0046437biological_processD-amino acid biosynthetic process
B0047810molecular_functionD-alanine-2-oxoglutarate aminotransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 900
ChainResidue
AARG98
AHIS100
BTYR31
BPLP585

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 901
ChainResidue
ATYR31
AHOH739
BARG98
BHIS100

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE PLP A 285
ChainResidue
AHIS47
AARG50
AARG138
ALYS145
ASER179
ASER180
ASER181
ALEU201
AGLY203
AILE204
ATHR205
ASER240
ATHR241
AHOH681
AHOH712
AHOH739
ATYR31

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PLP B 585
ChainResidue
AACT900
BTYR31
BHIS47
BARG50
BARG138
BSER180
BSER181
BGLY203
BILE204
BTHR205
BSER240
BTHR241
BLYS445
BHOH713
BHOH738
BHOH756

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"7626635","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9538014","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"7626635","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1daa
ChainResidueDetails
ALEU201
ALYS145
ASER177

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1daa
ChainResidueDetails
AILE144

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1daa
ChainResidueDetails
BILE144

site_idMCSA1
Number of Residues4
DetailsM-CSA 66
ChainResidueDetails
ATYR31electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
ALYS145covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
ASER177activator, electrostatic stabiliser, hydrogen bond acceptor
ALEU201steric role, van der waals interaction

site_idMCSA2
Number of Residues4
DetailsM-CSA 66
ChainResidueDetails
BTYR31electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
BLYS445covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
BSER177activator, electrostatic stabiliser, hydrogen bond acceptor
BLEU201steric role, van der waals interaction

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PDB entries from 2025-07-16

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