Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1G2W

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0008483molecular_functiontransaminase activity
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
A1901566biological_processorganonitrogen compound biosynthetic process
B0003824molecular_functioncatalytic activity
B0008483molecular_functiontransaminase activity
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
B1901566biological_processorganonitrogen compound biosynthetic process
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
DetailsACT_SITE: Proton acceptor => ECO:0000269|PubMed:7626635
ChainResidueDetails
ASER146
BSER146

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:9538014
ChainResidueDetails
AGLU32
BGLY178
ALEU51
AALA99
AGLN101
AGLY178
BGLU32
BLEU51
BALA99
BGLN101

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:7626635
ChainResidueDetails
ASER146
BSER146

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 66
ChainResidueDetails
AGLU32electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
ASER146covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
AGLY178activator, electrostatic stabiliser, hydrogen bond acceptor
ALYS202steric role, van der waals interaction

site_idMCSA2
Number of Residues4
DetailsM-CSA 66
ChainResidueDetails
BGLU32electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
BSER146covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor
BGLY178activator, electrostatic stabiliser, hydrogen bond acceptor
BLYS202steric role, van der waals interaction

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon