Structure of PDB 1maq Chain A Binding Site BS01

Receptor Information
>1maq Chain A (length=401) Species: 9031 (Gallus gallus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
SSWWSHVEMGPPDPILGVTEAFKRDTNSKKMNLGVGAYRDDNGKPYVLNC
VRKAEAMIAAKKMDKEYLPIAGLADFTRASAELALGENSEAFKSGRYVTV
QGISGTGSLRVGANFLQRFFKFSRDVYLPKPSWGNHTPIFRDAGLQLQAY
RYYDPKTCSLDFTGAMEDISKIPEKSIILLHACAHNPTGVDPRQEQWKEL
ASVVKKRNLLAYFDMAYQGFASGDINRDAWALRHFIEQGIDVVLSQSYAK
NMGLYGERAGAFTVICRDAEEAKRVESQLKILIRPMYSNPPMNGARIASL
ILNTPELRKEWLVEVKGMADRIISMRTQLVSNLKKEGSSHNWQHITDQIG
MFCFTGLKPEQVERLTKEFSIYMTKDGRISVAGVASSNVGYLAHAIHQVT
K
Ligand information
Ligand IDPGU
InChIInChI=1S/C13H19N2O9P/c1-7-12(18)9(8(4-14-7)6-24-25(21,22)23)5-15-10(13(19)20)2-3-11(16)17/h4,10,15,18H,2-3,5-6H2,1H3,(H,16,17)(H,19,20)(H2,21,22,23)/t10-/m0/s1
InChIKeyJMRKOGDJNHPMHS-JTQLQIEISA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)CNC(CCC(=O)O)C(=O)O)O
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(CN[CH](CCC(O)=O)C(O)=O)c1O
CACTVS 3.341Cc1ncc(CO[P](O)(O)=O)c(CN[C@@H](CCC(O)=O)C(O)=O)c1O
OpenEye OEToolkits 1.5.0Cc1c(c(c(cn1)COP(=O)(O)O)CN[C@@H](CCC(=O)O)C(=O)O)O
ACDLabs 10.04O=C(O)C(NCc1c(cnc(c1O)C)COP(=O)(O)O)CCC(=O)O
FormulaC13 H19 N2 O9 P
NameN-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-glutamic acid
ChEMBL
DrugBank
ZINCZINC000012501127
PDB chain1maq Chain A Residue 412 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1maq Crystal structures of true enzymatic reaction intermediates: aspartate and glutamate ketimines in aspartate aminotransferase.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		L18 S107 G108 T109 W140 N194 D222 Y225 S255 K258 R266 F360 R386
Binding residue
(residue number reindexed from 1)		L16 S104 G105 T106 W133 N186 D214 Y217 S247 K250 R258 F352 R378
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) W140 D222 A224 K258
Catalytic site (residue number reindexed from 1) W133 D214 A216 K250
Enzyme Commision number 2.6.1.1: aspartate transaminase.
2.6.1.7: kynurenine--oxoglutarate transaminase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004069 L-aspartate:2-oxoglutarate aminotransferase activity
GO:0008483 transaminase activity
GO:0016212 kynurenine-oxoglutarate transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0006103 2-oxoglutarate metabolic process
GO:0006520 amino acid metabolic process
GO:0006531 aspartate metabolic process
GO:0006533 aspartate catabolic process
GO:0006536 glutamate metabolic process
GO:0009058 biosynthetic 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:1maq, PDBe:1maq, PDBj:1maq
PDBsum1maq
PubMed7903048
UniProtP00508|AATM_CHICK Aspartate aminotransferase, mitochondrial (Gene Name=GOT2)

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