Structure of PDB 1bkg Chain B

Receptor sequence

>1bkgB (length=382) Species: 300852 (Thermus thermophilus HB8)

MRGLSRRVQAMKPSATVAVNAKALELRRQGVDLVALTAGEPDFDTPEHVK
EAARRALAQGKTKYAPPAGIPELREALAEKFRRENGLSVTPEETIVTVGG
KQALFNLFQAILDPGDEVIVLSPYWVSYPEMVRFAGGVVVEVETLPEEGF
VPDPERVRRAITPRTKALVVNSPNNPTGAVYPKEVLEALARLAVEHDFYL
VSDEIYEHLLYEGEHFSPGRVAPEHTLTVNGAAKAFAMTGWRIGYACGPK
EVIKAMASVSSQSTTSPDTIAQWATLEALTNQEASRAFVEMAREAYRRRR
DLLLEGLTALGLKAVRPSGAFYVLMDTSPIAPDEVRAAERLLEAGVAVVP
GTDFAAFGHVRLSYATSEENLRKALERFARVL

3D structure

• PDB: 1bkg Structure of Thermus thermophilus HB8 aspartate aminotransferase and its complex with maleate.
• Chain: B
• Resolution: 2.6 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): W125 D203 I205 K234
• Catalytic site (residue number reindexed from 1): W125 D203 I205 K234
• Enzyme Commision number: 2.6.1.1: aspartate transaminase.
  2.6.1.78: aspartate--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	PMP	B	G99 G100 K101 W125 N171 N175 D203 I205 Y206 K234 R242	G99 G100 K101 W125 N171 N175 D203 I205 Y206 K234 R242

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:0033853 aspartate-prephenate aminotransferase activity

Biological Process

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

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:1bkg, PDBe:1bkg, PDBj:1bkg
• PDBsum: 1bkg
• PubMed: 10029535
• UniProt: Q56232|AAPAT_THET8 Aspartate/prephenate aminotransferase (Gene Name=aspC)