Structure of PDB 5vwq Chain G

Receptor sequence

>5vwqG (length=396) Species: 83333 (Escherichia coli K-12)

MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDETGKTPVLTSVK
KAEQYLLENETTKNYLGIDGIPEFGRCTQELLFGKGSALINDKRARTAQT
PGGTGALRVAADFLAKNTSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYY
DAENHTLDFDALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL
SVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIVASSYSKNFGL
YNERVGACTLVAADSETVDRAFSQMKAAIRANYSNPPAHGASVVATILSN
DALRAIWEQELTDMRQRIQRMRQLFVNTLQEKGANRDFSFIIKQNGMFSF
SGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL

3D structure

• PDB: 5vwq Selective Targeting by a Mechanism-Based Inactivator against Pyridoxal 5'-Phosphate-Dependent Enzymes: Mechanisms of Inactivation and Alternative Turnover.
• Chain: G
• Resolution: 1.8 Å

Enzymatic activity

• 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	PMP	G	G103 T104 W130 D211 Y214 S243 S245 K246 R254	G103 T104 W130 D211 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
• 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

External links

• PDB: RCSB:5vwq, PDBe:5vwq, PDBj:5vwq
• PDBsum: 5vwq
• PubMed: 28816437
• UniProt: P00509|AAT_ECOLI Aspartate aminotransferase (Gene Name=aspC)