Structure of PDB 1art Chain A Binding Site BS02

Receptor Information
>1art 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 ID0A0
InChIInChI=1S/C5H9NO4/c1-5(6,4(9)10)2-3(7)8/h2,6H2,1H3,(H,7,8)(H,9,10)/t5-/m0/s1
InChIKeyCWAYDJFPMMUKOI-YFKPBYRVSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CC(CC(=O)O)(C(=O)O)N
CACTVS 3.341C[C@](N)(CC(O)=O)C(O)=O
CACTVS 3.341C[C](N)(CC(O)=O)C(O)=O
ACDLabs 10.04O=C(O)CC(N)(C(=O)O)C
OpenEye OEToolkits 1.5.0C[C@](CC(=O)O)(C(=O)O)N
FormulaC5 H9 N O4
Name2-methyl-L-aspartic acid
ChEMBL
DrugBank
ZINCZINC000002516276
PDB chain1art Chain A Residue 414 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1art X-ray crystallographic study of pyridoxal 5'-phosphate-type aspartate aminotransferases from Escherichia coli in open and closed form.
Resolution1.8 Å
Binding residue
(original residue number in PDB)		I37 G38 W140 Y225 R386
Binding residue
(residue number reindexed from 1)		I33 G34 W130 Y214 R374
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) W140 D222 A224 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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1art, PDBe:1art, PDBj:1art
PDBsum1art
PubMed7798192
UniProtP00509|AAT_ECOLI Aspartate aminotransferase (Gene Name=aspC)

[Back to BioLiP]