Structure of PDB 3ath Chain A Binding Site BS02

Receptor Information

>3ath Chain A (length=404) Species: 70601 (Pyrococcus horikoshii OT3)

SMLGDVERFFSKKALEMRASEVRELLKLVETSDIISLAGGLPNPKTFPKE
IIRDILVEIMEKYADKALQYGTTKGFTPLRETLMKWLGKRYGISQDNDIM
ITSGSQQALDLIGRVFLNPGDIVVVEAPTYLAALQAFNFYEPQYIQIPLD
DEGMKVEILEEKLKELKSQGKKVKVVYTVPTFQNPAGVTMNEDRRKYLLE
LASEYDFIVVEDDPYGELRYSGNPEKKIKALDNEGRVIYLGTFSKILAPG
FRIGWMVGDPGIIRKMEIAKQSTDLCTNVFGQVVAWRYVDGGYLEKHIPE
IRKFYKPRRDAMLEALEEFMPEGVKWTKPEGGMFIWVTLPDGIDSKKMLE
RAIKKGVAYVPGEAFYAHRDVKNTMRLNFTYVDEDKIMEGIKRLAETIKE
ELKA

Ligand information

• Ligand ID: AKG
• InChI: InChI=1S/C5H6O5/c6-3(5(9)10)1-2-4(7)8/h1-2H2,(H,7,8)(H,9,10)
• InChIKey: KPGXRSRHYNQIFN-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04: O=C(O)C(=O)CCC(=O)O
  OpenEye OEToolkits 1.7.6: C(CC(=O)O)C(=O)C(=O)O
  CACTVS 3.385: OC(=O)CCC(=O)C(O)=O
• Formula: C5 H6 O5
• Name: 2-OXOGLUTARIC ACID
• ChEMBL: CHEMBL1686
• DrugBank: DB08845
• ZINC: ZINC000001532519
• PDB chain: 3ath Chain A Residue 430

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3ath Characterization of kynurenine aminotransferase from hyperthermophilic archaeon: enzymatic activity for conversion to kynurenic acid is allosterically regulated by alpha-ketoglutaric acid cooperatively with kynurenine
• Resolution: 1.69 Å
• Binding residue (original residue number in PDB): D237 P238 Y239 G240 E241 Y263 G265 T266 I270 W279
• Binding residue (residue number reindexed from 1): D213 P214 Y215 G216 E217 Y239 G241 T242 I246 W255
• Annotation score: 5

Enzymatic activity

• Enzyme Commision number: 2.6.1.7: kynurenine--oxoglutarate transaminase.

Gene Ontology

Molecular Function

• GO:0008483 transaminase activity
• GO:0030170 pyridoxal phosphate binding

Biological Process

• GO:0009058 biosynthetic process
• GO:1901605 alpha-amino acid metabolic process

External links

• PDB: RCSB:3ath, PDBe:3ath, PDBj:3ath
• PDBsum: 3ath
• UniProt: O57946