Structure of PDB 1tog Chain B

Receptor sequence
>1togB (length=396) Species: 562 (Escherichia coli) [Search protein sequence]
MFENITATTADPILGLADLFRADERPGKIDLGIGVYKDETGKTPVLTSVK
KAEQYLLENETTKNYLGIDGIPEFGRCTQELLFGKGSALINDKRARTAQT
PGGSGALRVAADFLAKNTSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYY
DAENHTLDFDALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL
SVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIVASSYSKNFAL
YNERVGACTLVAADSETVDRAFGQMKAAIRDNYSSPPAHGASVVATILSN
DALRAIWEQELTDMRQRIQRMRQLFVNTLQEKGANRDFSFIIKQNGMFSF
SGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL
3D structure
PDB1tog Narrowing substrate specificity in a directly evolved enzyme: the A293D mutant of aspartate aminotransferase
ChainB
Resolution2.31 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 HCI B Y70 S296 Y65 S284 MOAD: Kd=0.6mM
PDBbind-CN: -logKd/Ki=3.22,Kd=0.6mM
BS02 HCI B L18 I37 G38 W140 X258 R386 L14 I33 G34 W130 X246 R374 MOAD: Kd=0.6mM
PDBbind-CN: -logKd/Ki=3.22,Kd=0.6mM
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:1tog, PDBe:1tog, PDBj:1tog
PDBsum1tog
PubMed15461450
UniProtP00509|AAT_ECOLI Aspartate aminotransferase (Gene Name=aspC)

[Back to BioLiP]