Structure of PDB 2ch1 Chain C

Receptor sequence
>2ch1C (length=388) Species: 7165 (Anopheles gambiae) [Search protein sequence]
KFTPPPASLRNPLIIPEKIMMGPGPSNCSKRVLTAMTNTVLSNFHAELFR
TMDEVKDGLRYIFQTENRATMCVSGSAHAGMEAMLSNLLEEGDRVLIAVN
GIWAERAVEMSERYGADVRTIEGPPDRPFSLETLARAIELHQPKCLFLTH
GDSSSGLLQPLEGVGQICHQHDCLLIVDAVASLCGVPFYMDKWEIDAVYT
GAQKVLGAPPGITPISISPKALDVIRNRRTKSKVFYWDLLLLGNYWGCYD
EPKRYHHTVASNLIFALREALAQIAEEGLENQIKRRIECAQILYEGLGKM
GLDIFVKDPRHRLPTVTGIMIPKGVDWWKVSQYAMNNFSLEVQGGLGPTF
GKAWRVGIMGECSTVQKIQFYLYGFKESLKATHPDYIF
3D structure
PDB2ch1 Crystal Structure of the Anopheles Gambiae 3-Hydroxykynurenine Transaminase
ChainC
Resolution2.4 Å
3D
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Enzymatic activity
Enzyme Commision number 2.6.1.44: alanine--glyoxylate transaminase.
2.6.1.63: kynurenine--glyoxylate 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 C Y256 T259 Y255 T258
BS02 PLP C S77 A78 H79 W104 S154 D179 V181 Q204 K205 S76 A77 H78 W103 S153 D178 V180 Q203 K204
Gene Ontology
Molecular Function
GO:0004760 L-serine-pyruvate transaminase activity
GO:0008453 alanine-glyoxylate transaminase activity
GO:0008483 transaminase activity
GO:0016740 transferase activity
GO:0030170 pyridoxal phosphate binding
GO:0047315 kynurenine-glyoxylate transaminase activity
Biological Process
GO:0009436 glyoxylate catabolic process
GO:0019265 glycine biosynthetic process, by transamination of glyoxylate
GO:0097053 L-kynurenine catabolic process
Cellular Component
GO:0005777 peroxisome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2ch1, PDBe:2ch1, PDBj:2ch1
PDBsum2ch1
PubMed16585514
UniProtQ7PRG3|HKT_ANOGA 3-hydroxykynurenine transaminase (Gene Name=HKT)

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