Structure of PDB 1spa Chain A Binding Site BS01

Receptor Information
>1spa Chain A (length=396) Species: 562 (Escherichia coli) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDETGKTPVLTSVK
KAEQYLLENETTKNYLGIDGIPEFGRCTQELLFGKGSALINDKRARTAQT
PGGTGALRVAADFLAKNTSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYY
DAENHTLDFDALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL
SVEKGWLPLFAFAYQGFARGLEEDAEGLRAFAAMHKELIVASSYSKNFGL
YNERVGACTLVAADSETVDRAFSQMKAAIRANYSNPPAHGASVVATILSN
DALRAIWEQELTDMRQRIQRMRQLFVNTLQEKGANRDFSFIIKQNGMFSF
SGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL
Ligand information
Ligand IDNPL
InChIInChI=1S/C9H15N2O5P/c1-6-9(12)8(3-10)7(4-11(6)2)5-16-17(13,14)15/h4H,3,5,10H2,1-2H3,(H2-,12,13,14,15)/p+1
InChIKeyBDHMQTZHNOSTBZ-UHFFFAOYSA-O
SMILES
SoftwareSMILES
CACTVS 3.341Cc1c(O)c(CN)c(CO[P](O)(O)=O)c[n+]1C
OpenEye OEToolkits 1.5.0Cc1c(c(c(c[n+]1C)COP(=O)(O)O)CN)O
ACDLabs 10.04O=P(O)(O)OCc1c[n+](c(c(O)c1CN)C)C
FormulaC9 H16 N2 O5 P
NameN-METHYL-4-DEOXY-4-AMINO-PYRIDOXAL-5-PHOSPHATE
ChEMBL
DrugBank
ZINCZINC000006232635
PDB chain1spa Chain A Residue 413 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1spa Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: the amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5'-phosphate.
Resolution2.0 Å
Binding residue
(original residue number in PDB)		G107 G108 T109 W140 H143 N194 A224 Y225 S255 S257 R266
Binding residue
(residue number reindexed from 1)		G102 G103 T104 W130 H133 N183 A213 Y214 S243 S245 R254
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) W140 A222 A224 K258
Catalytic site (residue number reindexed from 1) W130 A211 A213 K246
Enzyme Commision number 2.6.1.1: aspartate transaminase.
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004069 L-aspartate:2-oxoglutarate aminotransferase activity
GO:0004838 L-tyrosine-2-oxoglutarate transaminase activity
GO:0008483 transaminase activity
GO:0030170 pyridoxal phosphate binding
GO:0042802 identical protein binding
GO:0042803 protein homodimerization activity
Biological Process
GO:0006520 amino acid metabolic process
GO:0009058 biosynthetic process
GO:0009094 L-phenylalanine biosynthetic process
GO:0033585 L-phenylalanine biosynthetic process from chorismate via phenylpyruvate
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1spa, PDBe:1spa, PDBj:1spa
PDBsum1spa
PubMed1610831
UniProtP00509|AAT_ECOLI Aspartate aminotransferase (Gene Name=aspC)

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