Structure of PDB 4atq Chain B Binding Site BS03

Receptor Information
>4atq Chain B (length=442) Species: 290340 (Paenarthrobacter aurescens TC1) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LSYRIEQKRNINGAFPGPKSQALAERRSAVVAAGVASGVPVYVEDADGGI
IRDVDGNSFIDLGSGIAVTSVGASDPAVVAAVQEAAAHFTHTCFMVTPYE
GYVAVTEQLNRLTPGDHAKRTVLFNSGAEAVENAVKVARLATGRDAVVAF
DHAYHGRTNLTMALTAKAMPYKTNFGPFAPEVYRMPMSYPFREENPEITG
AEAAKRAITMIEKQIGGDQVAAIIIEPIQGEGGFIVPAEGFLPALSEWAK
EKGIVFIADEVQSGFCRTGEWFAVDHEGVVPDIITMAKGIAGGLPLSAIT
GRADLLDAVHPGGLGGTYGGNPVACAAALAAIDTMEQHDLNGRARHIEEL
ALGKLRELAAESVVGDIRGRGAMLAIELVQPGSKEPNAELTKAVAAACLK
EGVIILTCGTYGNVIRLLPPLVISDELLIDGLEVLAAAIKAH
Ligand information
Ligand IDABU
InChIInChI=1S/C4H9NO2/c5-3-1-2-4(6)7/h1-3,5H2,(H,6,7)
InChIKeyBTCSSZJGUNDROE-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.370NCCCC(O)=O
ACDLabs 12.01O=C(O)CCCN
OpenEye OEToolkits 1.7.0C(CC(=O)O)CN
FormulaC4 H9 N O2
NameGAMMA-AMINO-BUTANOIC ACID;
GAMMA(AMINO)-BUTYRIC ACID
ChEMBLCHEMBL96
DrugBankDB02530
ZINCZINC000001532620
PDB chain4atq Chain B Residue 1457 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4atq Structures of a Gamma-Aminobutyrate (Gaba) Transaminase from the S-Triazine-Degrading Organism Arthrobacter Aurescens Tc1 in Complex with Plp and with its External Aldimine Plp- Gaba Adduct.
Resolution2.75 Å
Binding residue
(original residue number in PDB)		Y161 R164 E238 K295
Binding residue
(residue number reindexed from 1)		Y154 R157 E231 K288
Annotation score5
Enzymatic activity
Catalytic site (original residue number in PDB) V42 Y161 E233 D266 Q269 K295 T324 R429
Catalytic site (residue number reindexed from 1) V35 Y154 E226 D259 Q262 K288 T317 R416
Enzyme Commision number 2.6.1.19: 4-aminobutyrate--2-oxoglutarate transaminase.
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0034386 4-aminobutyrate:2-oxoglutarate transaminase activity
GO:0042802 identical protein binding
Biological Process
GO:0009448 gamma-aminobutyric acid metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4atq, PDBe:4atq, PDBj:4atq
PDBsum4atq
PubMed23027742
UniProtA1R958

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