Structure of PDB 1ahg Chain B

Receptor sequence

>1ahgB (length=396) Species: 83333 (Escherichia coli K-12)

MFENITAAPADPILGLADLFRADERPGKINLGIGLYYDETGKIPVLTSVK
KAEQYLLENETTKLYLGIDGIPEFGRCTQELLFGKGSALINDKRARTAQT
PGGSGALRVAADFLAKNTSVKRVWVSNPSWPNHKSVFNSAGLEVREYAYY
DAENHTLDFDALINSLNEAQAGDVVLFHGCCHNPTGIDPTLEQWQTLAQL
SVEKGWLPLFDFAYQGFARGLEEDAEGLRAFAAMHKELIVASSYSKNFGL
YNERVGACTLVAADSETVDRAFSQMKAAIRANYSSPPAHGASVVATILSN
DALRAIWEQELTDMRQRIQRMRQLFVNTLQEKGANRDFSFIIKQNGMFSF
SGLTKEQVLRLREEFGVYAVASGRVNVAGMTPDNMAPLCEAIVAVL

3D structure

• PDB: 1ahg Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase.
• Chain: B
• Resolution: 2.5 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	TYR	B	D15 I17 L18 W140 R386	D11 I13 L14 W130 R374
BS02	PLP	B	G108 S109 W140 D222 S255 R266	G103 S104 W130 D211 S243 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:1ahg, PDBe:1ahg, PDBj:1ahg
• PDBsum: 1ahg
• PubMed: 7664122
• UniProt: P00509|AAT_ECOLI Aspartate aminotransferase (Gene Name=aspC)