Structure of PDB 3aov Chain A

Receptor sequence
>3aovA (length=404) Species: 70601 (Pyrococcus horikoshii OT3) [Search protein sequence]
SMLGDVERFFSKKALEMRASEVRELLKLVETSDIISLAGGLPNPKTFPKE
IIRDILVEIMEKYADKALQYGTTKGFTPLRETLMKWLGKRYGISQDNDIM
ITSGSQQALDLIGRVFLNPGDIVVVEAPTYLAALQAFNFYEPQYIQIPLD
DEGMKVEILEEKLKELKSQGKKVKVVYTVPTFQNPAGVTMNEDRRKYLLE
LASEYDFIVVEDDPYGELRYSGNPEKKIKALDNEGRVIYLGTFSKILAPG
FRIGWMVGDPGIIRKMEIAKQSTDLCTNVFGQVVAWRYVDGGYLEKHIPE
IRKFYKPRRDAMLEALEEFMPEGVKWTKPEGGMFIWVTLPDGIDSKKMLE
RAIKKGVAYVPGEAFYAHRDVKNTMRLNFTYVDEDKIMEGIKRLAETIKE
ELKA
3D structure
PDB3aov Characterization of kynurenine aminotransferase from hyperthermophilic archaeon: enzymatic activity for conversion to kynurenic acid is allosterically regulated by alpha-ketoglutaric acid cooperatively with kynurenine
ChainA
Resolution1.72 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.6.1.7: kynurenine--oxoglutarate transaminase.
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 A G128 S129 Q130 Y154 V203 N208 D236 P238 Y239 T266 S268 K269 R276 G104 S105 Q106 Y130 V179 N184 D212 P214 Y215 T242 S244 K245 R252
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

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Molecular Function
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Biological Process
External links
PDB RCSB:3aov, PDBe:3aov, PDBj:3aov
PDBsum3aov
PubMed
UniProtO57946

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