Structure of PDB 6f77 Chain D

Receptor sequence

>6f77D (length=399) Species: 266834 (Sinorhizobium meliloti 1021)

AFLADALSRVKPSATIAVSQKARELKAKGRDVIGLGAGEPDFDTPDNIKK
AAIDAIDRGETKYTPVSGIPELREAIAKKFKRENNLDYTAAQTIVGTGGK
QILFNAFMATLNPGDEVVIPAPYWVSYPEMVALCGGTPVFVPTRQENNFK
LKAEDLDRAITPKTKWFVFNSPSNPSGAAYSHEELKALTDVLMKHPHVWV
LTDDMYEHLTYGDFRFATPVEVEPGLYERTLTMNGVSKAYAMTGWRIGYA
AGPLHLIKAMDMIQGQQTSGAASIAQWAAVEALNGPQDFIGRNKEIFQGR
RDLVVSMLNQAKGISCPTPEGAFYVYPSCAGLIGKTAPSGKVIETDEDFV
SELLETEGVAVVHGSAFGLGPNFRISYATSEALLEEACRRIQRFCAACR

3D structure

• PDB: 6f77 Tyrosine metabolism: identification of a key residue in the acquisition of prephenate aminotransferase activity by 1 beta aspartate aminotransferase.
• Chain: D
• Resolution: 1.794 Å

Enzymatic activity

• Enzyme Commision number: 2.6.1.1: aspartate transaminase.
  2.6.1.79: glutamate--prephenate aminotransferase.

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	D	G99 G100 K101 W125 N171 N175 D204 M206 Y207 S239 K240 R248	G98 G99 K100 W124 N170 N174 D203 M205 Y206 S237 K238 R246

Gene Ontology

Molecular Function

• GO:0003824 catalytic activity
• GO:0004069 L-aspartate:2-oxoglutarate aminotransferase activity
• GO:0008483 transaminase activity
• GO:0030170 pyridoxal phosphate binding
• GO:0033854 glutamate-prephenate aminotransferase activity

Biological Process

• GO:0006520 amino acid metabolic process
• GO:0009058 biosynthetic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:6f77, PDBe:6f77, PDBj:6f77
• PDBsum: 6f77
• PubMed: 30771275
• UniProt: Q02635|AAPAT_RHIME Aspartate/prephenate aminotransferase (Gene Name=aatA)