Structure of PDB 3pa9 Chain A

Receptor sequence
>3pa9A (length=396) Species: 562 (Escherichia coli) [Search protein sequence]
MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDETGKTPVLTSVK
KAEQYLLENETTKNYLGIDGIPEFGRCTQELLFGKGSALINDKRARTAQT
PGGTGALRVAADFLAKNTSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYY
DAENHTLDFDALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL
SVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIVASSYSKNFGL
YNERVGACTLVAADSETVDRAFSQMKAAIRANYSNPPAHGASVVATILSN
DALRAIWEQELTDMRQRIQRMRQLFVNTLQEKGANRDFSFIIKQNGMFSF
SGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL
3D structure
PDB3pa9 Mechanism of inactivation of Escherichia coli aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-furancarboxylic acid .
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) W130 D211 A213 K246
Catalytic site (residue number reindexed from 1) W130 D211 A213 K246
Enzyme Commision number 2.6.1.-
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 PJ7 A G34 W130 K246 F348 R374 G34 W130 K246 F348 R374
BS02 PMP A G103 T104 W130 D211 A213 Y214 S243 S245 K246 R254 G103 T104 W130 D211 A213 Y214 S243 S245 K246 R254
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
Biological Process
GO:0006520 amino acid metabolic process
GO:0009058 biosynthetic process
GO:0033585 L-phenylalanine biosynthetic process from chorismate via phenylpyruvate
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:3pa9, PDBe:3pa9, PDBj:3pa9
PDBsum3pa9
PubMed21033689
UniProtD3H0F7

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