Structure of PDB 2d64 Chain A

Receptor sequence
>2d64A (length=396) Species: 562 (Escherichia coli) [Search protein sequence]
MFENITTAPADPILGLADLLRADERPGKIDLGMGVYNDETGKTPVLTSVK
KAEQYLLENETTKNYLGIDGIPEFGRCTQELLFGKGSALINDKRARTAQT
PGGTGALRVAADFLAKNTSVKRVWVSNPGWPTHKSVFNSAGLEVREYAYY
DAENHTLDFDALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL
SVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIVASSYSKNFGL
YNERVGACTLVAADSETVDRAFSQMKAAIRVNYSSPPAHGASVVATILSN
DALRAIWEQELTDMRQRIQRMRQLFVNTLQEKGANRDFSFTIKQNGMFFF
GGLTKEQVLRLREEFGVYAVASGRLNVAGMTPDNLAPLCEAIVAVL
3D structure
PDB2d64 The Structures of Aspartate Aminotransferase with Mutations of Non-Active-Site Residues
ChainA
Resolution2.05 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.-
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 PLP A G107 G108 T109 W140 N194 D222 A224 Y225 S255 S257 K258 R266 G102 G103 T104 W130 N183 D211 A213 Y214 S243 S245 K246 R254
BS02 IVA A I17 M37 G38 W140 R386 I13 M33 G34 W130 R374
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:2d64, PDBe:2d64, PDBj:2d64
PDBsum2d64
PubMed
UniProtQ304P7

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