Structure of PDB 5bj3 Chain B

Receptor sequence

>5bj3B (length=363) Species: 271 (Thermus aquaticus)

MRGLSRRVQAMKPLVALTAGEPDFDTPEHVKEAARRALAQGKTKYAPPAG
IPELREALAEKFRRENGLSVTPEETIVTVGGSQALFNLFQAILDPGDEVI
VLSPYWVSYPEMVRFAGGVVVEVETLPEEGFVPDPERVRRAITPRTKALV
VNSPNNPTGAVYPKEVLEALARLAVEHDFYLVSDEIYEHLLYEGEHFSPG
RVAPEHTLTVNGAAKAFAMTGWRIGYACGPKEVIKAMASVSRQSTTSPDT
IAQWATLEALTNQEASRAFVEMAREAYRRRRDLLLEGLTALGLKAVRPSG
AFYVLMDTSPIAPDEVRAAERLLEAGVAVVPGTDFAAFGHVRLSYATSEE
NLRKALERFARVL

3D structure

• PDB: 5bj3 Substrate recognition mechanism of thermophilic dual-substrate enzyme
• Chain: B
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): W125 D203 I205 K234
• Catalytic site (residue number reindexed from 1): W106 D184 I186 K215
• 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	PLP	B	G99 G100 S101 W125 N175 D203 I205 Y206 A233 K234 R242	G80 G81 S82 W106 N156 D184 I186 Y187 A214 K215 R223

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:5bj3, PDBe:5bj3, PDBj:5bj3
• PDBsum: 5bj3
• PubMed: 11432784
• UniProt: Q56232|AAPAT_THET8 Aspartate/prephenate aminotransferase (Gene Name=aspC)