Structure of PDB 1gck Chain B

Receptor sequence

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

MRGLSRRVQAMKPSATVAVNAKALELRRQGVDLVALTAGEPDFDTPEHVK
EAARRALAQGKTKYAPPAGIPELREALAEKFRRENGLSVTPEETIVTVGG
SQALFNLFQAILDPGDEVIVLSPYWVSYPEMVRFAGGVVVEVETLPEEGF
VPDPERVRRAITPRTKALVVNSPNNPTGAVYPKEVLEALARLAVEHDFYL
VSDEIYEHLLYEGEHFSPGRVAPEHTLTVNGAAKAFAMTGWRIGYACGPK
EVIKAMASVSRQSTTSPDTIAQWATLEALTNQEASRAFVEMAREAYRRRR
DLLLEGLTALGLKAVRPSGAFYVLMDTSPIAPDEVRAAERLLEAGVAVVP
GTDFAAFGHVRLSYATSEENLRKALERFARVL

3D structure

• PDB: 1gck Substrate recognition mechanism of thermophilic dual-substrate enzyme.
• Chain: B
• Resolution: 2.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): W625 D703 I705 K734
• 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	ASP	B	Y564 R761	Y64 R261
BS02	ASP	B	T516 G539 W625 N675 Y822 R861	T16 G39 W125 N175 Y322 R361
BS03	PLP	B	G599 G600 S601 W625 D703 I705 Y706 R742	G99 G100 S101 W125 D203 I205 Y206 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:1gck, PDBe:1gck, PDBj:1gck
• PDBsum: 1gck
• PubMed: 11432784
• UniProt: Q56232|AAPAT_THET8 Aspartate/prephenate aminotransferase (Gene Name=aspC)