Structure of PDB 1gc3 Chain B

Receptor sequence

>1gc3B (length=382) Species: 300852 (Thermus thermophilus HB8)

MRGLSRRVQAMKPDAVVAVNAKALELRRQGVDLVALTAGEPDFDTPEHVK
EAARRALAQGKTKYAPPAGIPELREALAEKFRRENGLSVTPEETIVTVGG
SQALFNLFQAILDPGDEVIVLSPYWVSYPEMVRFAGGVVVEVETLPEEGF
VPDPERVRRAITPRTKALVVNSPNNPTGAVYPKEVLEALARLAVEHDFYL
VSDEIYEHLLYEGEHFSPGRVAPEHTLTVNGAAKAFAMTGWRIGYACGPK
EVIKAMASVSRQSTTSPDTIAQWATLEALTNQEASRAFVEMAREAYRRRR
DLLLEGLTALGLKAVRPSGAFYVLMDTSPIAPDEVRAAERLLEAGVAVVP
GTDFAAFGHVRLSYATSEENLRKALERFARVL

3D structure

• PDB: 1gc3 Substrate recognition mechanism of thermophilic dual-substrate enzyme.
• Chain: B
• Resolution: 3.3 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	TRP	B	V516 G539 K734 Y822 R861	V16 G39 K234 Y322 R361
BS02	PLP	B	G600 S601 W625 N675 D703 Y706 K734 R742	G100 S101 W125 N175 D203 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:1gc3, PDBe:1gc3, PDBj:1gc3
• PDBsum: 1gc3
• PubMed: 11432784
• UniProt: Q56232|AAPAT_THET8 Aspartate/prephenate aminotransferase (Gene Name=aspC)