Structure of PDB 1bjw Chain A Binding Site BS01

Receptor Information
>1bjw Chain A (length=382) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MRGLSRRVQAMKPSATVAVNAKALELRRQGVDLVALTAGEPDFDTPEHVK
EAARRALAQGKTKYAPPAGIPELREALAEKFRRENGLSVTPEETIVTVGG
KQALFNLFQAILDPGDEVIVLSPYWVSYPEMVRFAGGVVVEVETLPEEGF
VPDPERVRRAITPRTKALVVNSPNNPTGAVYPKEVLEALARLAVEHDFYL
VSDEIYEHLLYEGEHFSPGRVAPEHTLTVNGAAKAFAMTGWRIGYACGPK
EVIKAMASVSSQSTTSPDTIAQWATLEALTNQEASRAFVEMAREAYRRRR
DLLLEGLTALGLKAVRPSGAFYVLMDTSPIAPDEVRAAERLLEAGVAVVP
GTDFAAFGHVRLSYATSEENLRKALERFARVL
Ligand information
Ligand IDPO4
InChIInChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChIKeyNBIIXXVUZAFLBC-UHFFFAOYSA-K
SMILES
SoftwareSMILES
CACTVS 3.341[O-][P]([O-])([O-])=O
ACDLabs 10.04[O-]P([O-])([O-])=O
OpenEye OEToolkits 1.5.0[O-]P(=O)([O-])[O-]
FormulaO4 P
NamePHOSPHATE ION
ChEMBL
DrugBankDB14523
ZINC
PDB chain1bjw Chain A Residue 414 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1bjw Structure of Thermus thermophilus HB8 aspartate aminotransferase and its complex with maleate.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		G39 W125 N175 R361
Binding residue
(residue number reindexed from 1)		G39 W125 N175 R361
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) W125 D203 I205 K234
Catalytic site (residue number reindexed from 1) W125 D203 I205 K234
Enzyme Commision number 2.6.1.1: aspartate transaminase.
2.6.1.78: aspartate--prephenate aminotransferase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004069 L-aspartate:2-oxoglutarate aminotransferase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0033853 aspartate-prephenate aminotransferase activity
Biological Process
GO:0006520 amino acid metabolic process
GO:0009058 biosynthetic process
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1bjw, PDBe:1bjw, PDBj:1bjw
PDBsum1bjw
PubMed10029535
UniProtQ56232|AAPAT_THET8 Aspartate/prephenate aminotransferase (Gene Name=aspC)

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