Structure of PDB 3av7 Chain C

Receptor sequence
>3av7C (length=404) Species: 70601 (Pyrococcus horikoshii OT3) [Search protein sequence]
SMLGDVERFFSKKALEMRASEVRELLKLVETSDIISLAGGLPNPKTFPKE
IIRDILVEIMEKYADKALQYGTTKGFTPLRETLMKWLGKRYGISQDNDIM
ITSGSQQALDLIGRVFLNPGDIVVVEAPTYLAALQAFNFYEPQYIQIPLD
DEGMKVEILEEKLKELKSQGKKVKVVYTVPTFQNPAGVTMNEDRRKYLLE
LASEYDFIVVEDDPYGELRYSGNPEKKIKALDNEGRVIYLGTFSKILAPG
FRIGWMVGDPGIIRKMEIAKQSTDLCTNVFGQVVAWRYVDGGYLEKHIPE
IRKFYKPRRDAMLEALEEFMPEGVKWTKPEGGMFIWVTLPDGIDSKKMLE
RAIKKGVAYVPGEAFYAHRDVKNTMRLNFTYVDEDKIMEGIKRLAETIKE
ELKA
3D structure
PDB3av7 Structural insight into kynurenic acid excretion mechanisms of kynurenine aminotransferase in the hyperthermophilic archaeon Pyrococcus horikoshii
ChainC
Resolution1.84 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 PMP C G128 S129 Q130 Y154 N208 D236 P238 Y239 T266 S268 K269 R276 G104 S105 Q106 Y130 N184 D212 P214 Y215 T242 S244 K245 R252
BS02 KYN C G64 Y154 N208 F389 R400 G40 Y130 N184 F365 R376
BS03 KYA C S44 V46 R47 L155 Q159 A388 R393 S20 V22 R23 L131 Q135 A364 R369
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:3av7, PDBe:3av7, PDBj:3av7
PDBsum3av7
PubMed
UniProtO57946

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