Structure of PDB 2ch2 Chain C

Receptor sequence
>2ch2C (length=387) Species: 7165 (Anopheles gambiae) [Search protein sequence]
FTPPPASLRNPLIIPEKIMMGPGPSNCSKRVLTAMTNTVLSNFHAELFRT
MDEVKDGLRYIFQTENRATMCVSGSAHAGMEAMLSNLLEEGDRVLIAVNG
IWAERAVEMSERYGADVRTIEGPPDRPFSLETLARAIELHQPKCLFLTHG
DSSSGLLQPLEGVGQICHQHDCLLIVDAVASLCGVPFYMDKWEIDAVYTG
AQKVLGAPPGITPISISPKALDVIRNRRTKSKVFYWDLLLLGNYWGCYDE
PKRYHHTVASNLIFALREALAQIAEEGLENQIKRRIECAQILYEGLGKMG
LDIFVKDPRHRLPTVTGIMIPKGVDWWKVSQYAMNNFSLEVQGGLGPTFG
KAWRVGIMGECSTVQKIQFYLYGFKESLKATHPDYIF
3D structure
PDB2ch2 Crystal Structure of the Anopheles Gambiae 3-Hydroxykynurenine Transaminase
ChainC
Resolution2.7 Å
3D
structure
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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 Y254 T257
BS02 KY1 C G25 W104 Q344 R356 G23 W102 Q342 R354
BS03 KY1 C N44 F45 Y256 N42 F43 Y254
BS04 PLP C S77 A78 H79 W104 S154 D179 V181 K205 S75 A76 H77 W102 S152 D177 V179 K203
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:2ch2, PDBe:2ch2, PDBj:2ch2
PDBsum2ch2
PubMed16585514
UniProtQ7PRG3|HKT_ANOGA 3-hydroxykynurenine transaminase (Gene Name=HKT)

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