Structure of PDB 1ahf Chain A Binding Site BS02
Receptor Information
>1ahf Chain A (length=396) Species:
562
(Escherichia coli) [
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MFENITAAPADPILGLADLFRADERPGKINLGIGLYYDETGKIPVLTSVK
KAEQYLLENETTKLYLGIDGIPEFGRCTQELLFGKGSALINDKRARTAQT
PGGSGALRVAADFLAKNTSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYY
DAENHTLDFDALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL
SVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIVASSYSKNFGL
YNERVGACTLVAADSETVDRAFSQMKAAIRANYSSPPAHGASVVATILSN
DALRAIWEQELTDMRQRIQRMRQLFVNTLQEKGANRDFSFIIKQNGMFSF
SGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL
Ligand information
Ligand ID
IOP
InChI
InChI=1S/C11H11NO2/c13-11(14)6-5-8-7-12-10-4-2-1-3-9(8)10/h1-4,7,12H,5-6H2,(H,13,14)
InChIKey
GOLXRNDWAUTYKT-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
O=C(O)CCc2c1ccccc1nc2
OpenEye OEToolkits 1.5.0
c1ccc2c(c1)c(c[nH]2)CCC(=O)O
CACTVS 3.341
OC(=O)CCc1c[nH]c2ccccc12
Formula
C11 H11 N O2
Name
INDOLYLPROPIONIC ACID
ChEMBL
CHEMBL207225
DrugBank
DB02758
ZINC
ZINC000000007700
PDB chain
1ahf Chain A Residue 411 [
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Receptor-Ligand Complex Structure
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PDB
1ahf
Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase.
Resolution
2.3 Å
Binding residue
(original residue number in PDB)
I17 L18 I37 G38 W140 R386
Binding residue
(residue number reindexed from 1)
I13 L14 I33 G34 W130 R374
Annotation score
1
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
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Molecular Function
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Cellular Component
External links
PDB
RCSB:1ahf
,
PDBe:1ahf
,
PDBj:1ahf
PDBsum
1ahf
PubMed
7664122
UniProt
P00509
|AAT_ECOLI Aspartate aminotransferase (Gene Name=aspC)
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