Structure of PDB 1ahg Chain A Binding Site BS01
Receptor Information
>1ahg Chain A (length=396) Species:
83333
(Escherichia coli K-12) [
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MFENITAAPADPILGLADLFRADERPGKINLGIGLYYDETGKIPVLTSVK
KAEQYLLENETTKLYLGIDGIPEFGRCTQELLFGKGSALINDKRARTAQT
PGGSGALRVAADFLAKNTSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYY
DAENHTLDFDALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL
SVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIVASSYSKNFGL
YNERVGACTLVAADSETVDRAFSQMKAAIRANYSSPPAHGASVVATILSN
DALRAIWEQELTDMRQRIQRMRQLFVNTLQEKGANRDFSFIIKQNGMFSF
SGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL
Ligand information
Ligand ID
TYR
InChI
InChI=1S/C9H11NO3/c10-8(9(12)13)5-6-1-3-7(11)4-2-6/h1-4,8,11H,5,10H2,(H,12,13)/t8-/m0/s1
InChIKey
OUYCCCASQSFEME-QMMMGPOBSA-N
SMILES
Software
SMILES
ACDLabs 10.04
O=C(O)C(N)Cc1ccc(O)cc1
OpenEye OEToolkits 1.5.0
c1cc(ccc1C[C@@H](C(=O)O)N)O
OpenEye OEToolkits 1.5.0
c1cc(ccc1CC(C(=O)O)N)O
CACTVS 3.341
N[CH](Cc1ccc(O)cc1)C(O)=O
CACTVS 3.341
N[C@@H](Cc1ccc(O)cc1)C(O)=O
Formula
C9 H11 N O3
Name
TYROSINE
ChEMBL
CHEMBL925
DrugBank
DB00135
ZINC
ZINC000000266964
PDB chain
1ahg Chain A Residue 501 [
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Receptor-Ligand Complex Structure
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PDB
1ahg
Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase.
Resolution
2.5 Å
Binding residue
(original residue number in PDB)
D15 I17 L18 W140 R386
Binding residue
(residue number reindexed from 1)
D11 I13 L14 W130 R374
Annotation score
2
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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Biological Process
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Cellular Component
External links
PDB
RCSB:1ahg
,
PDBe:1ahg
,
PDBj:1ahg
PDBsum
1ahg
PubMed
7664122
UniProt
P00509
|AAT_ECOLI Aspartate aminotransferase (Gene Name=aspC)
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