Structure of PDB 2q7w Chain A

Receptor sequence
>2q7wA (length=379) Species: 562 (Escherichia coli) [Search protein sequence]
MFENITAAPAKINLGIGVYKDETGKTPVLTSVKKAEQYLLENETTKNYLG
IDGIPEFGRCTQELLFGKGSALINDKRARTAQTPGGTGALRVAADFLAKN
TSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYYDAENHTLDFDALINSLN
EAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQLSVEKGWLPLFDFAYQGF
ARGLEEDAEGLRAFAAMHKELIVASSYSKNFGLYNERVGACTLVAADSET
VDRAFSQMKAAIRANYSNPPAHGASVVATILSNDALRAIWEQELTDMRQR
IQRMRQLFVNTLQEKGANRDFSFIIKQNGMFSFSGLTKEQVLRLREEFGV
YAVASGRVNVAGMTPDNMAPLCEAIVAVL
3D structure
PDB2q7w Inactivation of Escherichia coli l-Aspartate Aminotransferase by (S)-4-Amino-4,5-dihydro-2-thiophenecarboxylic Acid Reveals "A Tale of Two Mechanisms".
ChainA
Resolution1.4 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) W113 D194 A196 K229
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 PSZ A G34 G103 T104 W130 N183 D211 Y214 S243 S245 X246 R254 F348 R374 G17 G86 T87 W113 N166 D194 Y197 S226 S228 X229 R237 F331 R357
BS02 PMP A G103 T104 W130 D211 Y214 S243 S245 X246 R254 G86 T87 W113 D194 Y197 S226 S228 X229 R237
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:2q7w, PDBe:2q7w, PDBj:2q7w
PDBsum2q7w
PubMed17713924
UniProtP00509|AAT_ECOLI Aspartate aminotransferase (Gene Name=aspC)

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