Structure of PDB 1asd Chain A Binding Site BS01

Receptor Information
>1asd 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
SVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIVASSYSKNFGL
YNERVGACTLVAADSETVDRAFSQMKAAIRANYSNPPAHGASVVATILSN
DALRAIWEQELTDMRQRIQRMRQLFVNTLQEKGANRDFSFIIKQNGMFSF
SGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL
Ligand information
Ligand IDMPL
InChIInChI=1S/C9H12NO6P/c1-6-9(12)8(4-11)7(3-10(6)2)5-16-17(13,14)15/h3-4H,5H2,1-2H3,(H2-,11,12,13,14,15)/p+1
InChIKeyCBNMAKRKGWDQHB-UHFFFAOYSA-O
SMILES
SoftwareSMILES
CACTVS 3.341Cc1c(O)c(C=O)c(CO[P](O)(O)=O)c[n+]1C
ACDLabs 10.04O=P(O)(O)OCc1c[n+](c(c(O)c1C=O)C)C
OpenEye OEToolkits 1.5.0Cc1c(c(c(c[n+]1C)COP(=O)(O)O)C=O)O
FormulaC9 H13 N O6 P
NameN-METHYL-PYRIDOXAL-5'-PHOSPHATE
ChEMBL
DrugBankDB01639
ZINCZINC000012500943
PDB chain1asd Chain A Residue 409 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB1asd 2.8 Angstroms Resolution Crystal Structure of an Active Site Mutant of Aspartate Aminotransferase from Escherichia Coli
Resolution2.2 Å
Binding residue
(original residue number in PDB)		G114 G115 T116 W142 N195 D223 A225 Y226 S255 S257 K258 R266
Binding residue
(residue number reindexed from 1)		G102 G103 T104 W130 N183 D211 A213 Y214 S243 S245 K246 R254
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) W142 D223 A225 K258
Catalytic site (residue number reindexed from 1) W130 D211 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:1asd, PDBe:1asd, PDBj:1asd
PDBsum1asd
PubMed
UniProtP00509|AAT_ECOLI Aspartate aminotransferase (Gene Name=aspC)

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