Structure of PDB 5bj4 Chain B

Receptor sequence

>5bj4B (length=366) Species: 300852 (Thermus thermophilus HB8)

MRGLSRRVQAMKPGVDLVALTAGEPDFDTPEHVKEAARRALAQGKTKYAP
PAGIPELREALAEKFRRENGLSVTPEETIVTVGGSQALFNLFQAILDPGD
EVIVLSPYWVSYPEMVRFAGGVVVEVETLPEEGFVPDPERVRRAITPRTK
ALVVNSPNNPTGAVYPKEVLEALARLAVEHDFYLVSDEIYEHLLYEGEHF
SPGRVAPEHTLTVNGAAKAFAMTGWRIGYACGPKEVIKAMASVSRQSTTS
PDTIAQWATLEALTNQEASRAFVEMAREAYRRRRDLLLEGLTALGLKAVR
PSGAFYVLMDTSPIAPDEVRAAERLLEAGVAVVPGTDFAAFGHVRLSYAT
SEENLRKALERFARVL

3D structure

• PDB: 5bj4 Substrate recognition mechanism of thermophilic dual-substrate enzyme
• Chain: B
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): W125 D203 I205 K234
• Catalytic site (residue number reindexed from 1): W109 D187 I189 K218
• 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	G83 G84 S85 W109 N159 D187 I189 Y190 A217 K218 R226

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:5bj4, PDBe:5bj4, PDBj:5bj4
• PDBsum: 5bj4
• PubMed: 11432784
• UniProt: Q56232|AAPAT_THET8 Aspartate/prephenate aminotransferase (Gene Name=aspC)