Structure of PDB 3aat Chain A

Receptor sequence

>3aatA (length=396) Species: 562 (Escherichia coli)

MFENITAAPADPILGLADLFRADERPGKINLGIGVYKDETGKTPVLTSVK
KAEQYLLENETTKNYLGIDGIPEFGRCTQELLFGKGSALINDKRARTAQT
PGGTGALRVAADFLAKNTSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYY
DAENHTLDFDALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL
SVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIVASSYSKNFGL
YNERVGACTLVAADSETVDRAFSQMKAAIRANYSNPPAHGASVVATILSN
DALRAIWEQELTDMRQRIQRMRQLFVNTLQEKGANRDFSFIIKQNGMFSF
SGLTKEQVLRLREEFGVYAVASGFVNVAGMTPDNMAPLCEAIVAVL

3D structure

• PDB: 3aat Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase.
• Chain: A
• Resolution: 2.8 Å

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	PLP	A	G107 G108 T109 W140 N194 D222 Y225 S255 K258 R266	G102 G103 T104 W130 N183 D211 Y214 S243 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:3aat, PDBe:3aat, PDBj:3aat
• PDBsum: 3aat
• PubMed: 1993208
• UniProt: P00509|AAT_ECOLI Aspartate aminotransferase (Gene Name=aspC)