Structure of PDB 1akc Chain A Binding Site BS01

Receptor Information
>1akc 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
ASVVKKRNLLAYFDMAYQGFASGDINRDAWALRHFIEQGIDVVLSQSYAH
NMGLYGERAGAFTVICRDAEEAKRVESQLKILIRPMYSNPPMNGARIASL
ILNTPELRKEWLVEVKGMADRIISMRTQLVSNLKKEGSSHNWQHITDQIG
MFCFTGLKPEQVERLTKEFSIYMTKDGRISVAGVASSNVGYLAHAIHQVT
K
Ligand information
Ligand IDPPE
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)/p+1/t10-/m0/s1
InChIKeyJMRKOGDJNHPMHS-JTQLQIEISA-O
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0Cc1c(c(c(c[nH+]1)COP(=O)(O)O)CN[C@@H](CCC(=O)O)C(=O)O)O
CACTVS 3.341Cc1[nH+]cc(CO[P](O)(O)=O)c(CN[CH](CCC(O)=O)C(O)=O)c1O
CACTVS 3.341Cc1[nH+]cc(CO[P](O)(O)=O)c(CN[C@@H](CCC(O)=O)C(O)=O)c1O
OpenEye OEToolkits 1.5.0Cc1c(c(c(c[nH+]1)COP(=O)(O)O)CNC(CCC(=O)O)C(=O)O)O
ACDLabs 10.04O=C(O)C(NCc1c(c[nH+]c(c1O)C)COP(=O)(O)O)CCC(=O)O
FormulaC13 H20 N2 O9 P
Name4-[(1,3-DICARBOXY-PROPYLAMINO)-METHYL]-3-HYDROXY-2-METHYL-5-PHOSPHONOOXYMETHYL-PYRIDINIUM;
PYRIDOXYL-GLUTAMIC ACID-5'-MONOPHOSPHATE
ChEMBL
DrugBankDB01813
ZINC
PDB chain1akc Chain A Residue 411 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1akc Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking the pyridoxal 5'-phosphate-binding lysine residue.
Resolution2.3 Å
Binding residue
(original residue number in PDB)		V37 G38 S107 G108 T109 W140 N194 D222 A224 Y225 S255 R266 R386
Binding residue
(residue number reindexed from 1)		V35 G36 S104 G105 T106 W133 N186 D214 A216 Y217 S247 R258 R378
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) W140 D222 A224 H258
Catalytic site (residue number reindexed from 1) W133 D214 A216 H250
Enzyme Commision number 2.6.1.1: aspartate transaminase.
2.6.1.7: kynurenine--oxoglutarate transaminase.
Gene Ontology
Molecular Function
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:1akc, PDBe:1akc, PDBj:1akc
PDBsum1akc
PubMed7819232
UniProtP00508|AATM_CHICK Aspartate aminotransferase, mitochondrial (Gene Name=GOT2)

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