Structure of PDB 2xh1 Chain B Binding Site BS02

Receptor Information
>2xh1 Chain B (length=412) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ENYARFITAASAARNPSPIMISLAGGLPNPNMFPFKTAVITVENGKTIQF
GEEMMKRALQYSPSAGIPELLSWLKQLQIKLHNPPTIHYPPSQGQMDLCV
TSGSQQGLCKVFEMIINPGDNVLLDEPAYSGTLQSLHPLGCNIINVASDE
SGIVPDSLRDILSRWKPEDAKNPQKNTPKFLYTVPNGNNPTGNSLTSERK
KEIYELARKYDFLIIEDDPYYFLQFNKFRVPTFLSMDVDGRVIRADSFSK
IISSGLRIGFLTGPKPLIERVILHIQVSTLHPSTFNQLMISQLLHEWGEE
GFMAHVDRVIDFYSNQKDAILAAADKWLTGLAEWHVPAAGMFLWIKVKGI
NDVKELIEEKAVKMGVLMLPGNAFYVDSSAPSPYLRASFSSASPEQMDVA
FQVLAQLIKESL
Ligand information
Ligand IDPLP
InChIInChI=1S/C8H10NO6P/c1-5-8(11)7(3-10)6(2-9-5)4-15-16(12,13)14/h2-3,11H,4H2,1H3,(H2,12,13,14)
InChIKeyNGVDGCNFYWLIFO-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(C=O)c1O
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)C=O)O
ACDLabs 10.04O=P(O)(O)OCc1cnc(c(O)c1C=O)C
FormulaC8 H10 N O6 P
NamePYRIDOXAL-5'-PHOSPHATE;
VITAMIN B6 Phosphate
ChEMBLCHEMBL82202
DrugBankDB00114
ZINCZINC000001532514
PDB chain2xh1 Chain B Residue 1427 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2xh1 Crystal Structure-Based Selective Targeting of the Pyridoxal 5'-Phsosphate Dependent Enzyme Kynurenine Aminotransferase II for Cognitive Enhancement
Resolution2.1 Å
Binding residue
(original residue number in PDB)		S117 Q118 Y142 D230 P232 Y233 S260 S262 R270
Binding residue
(residue number reindexed from 1)		S104 Q105 Y129 D217 P219 Y220 S247 S249 R257
Annotation score1
Enzymatic activity
Enzyme Commision number 2.6.1.39: 2-aminoadipate transaminase.
2.6.1.4: glycine transaminase.
2.6.1.63: kynurenine--glyoxylate transaminase.
2.6.1.7: kynurenine--oxoglutarate transaminase.
2.6.1.73: methionine--glyoxylate transaminase.
Gene Ontology
Molecular Function
GO:0008483 transaminase activity
GO:0016212 kynurenine-oxoglutarate transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0042803 protein homodimerization activity
GO:0047315 kynurenine-glyoxylate transaminase activity
GO:0047536 2-aminoadipate transaminase activity
GO:0047958 glycine:2-oxoglutarate aminotransferase activity
GO:0050094 methionine-glyoxylate transaminase activity
Biological Process
GO:0006103 2-oxoglutarate metabolic process
GO:0006536 glutamate metabolic process
GO:0009058 biosynthetic process
GO:0033512 L-lysine catabolic process to acetyl-CoA via saccharopine
GO:0070189 kynurenine metabolic process
GO:1901605 alpha-amino acid metabolic process
Cellular Component
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2xh1, PDBe:2xh1, PDBj:2xh1
PDBsum2xh1
PubMed20684605
UniProtQ8N5Z0|AADAT_HUMAN Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial (Gene Name=AADAT)

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