Structure of PDB 2qhx Chain B

Receptor sequence
>2qhxB (length=265) Species: 5664 (Leishmania major) [Search protein sequence]
TVPVALVTGAAKRLGRSIAEGLHAEGYAVCLHYHRSAAEANALSATLNAR
RPNSAITVQADLSNVATAPSAPVTLFTRCAELVAACYTHWGRCDVLVNNA
SSFYPTPLLREAMETATADLFGSNAIAPYFLIKAFAHRVAGTPAKHRGTN
YSIINMVDAMTNQPLLGYTIYTMAKGALEGLTRSAALELAPLQIRVNGVG
PGLSVLVDDMPPAVWEGHRSKVPLYQRDSSAAEVSDVVIFLCSSKAKYIT
GTCVKVDGGYSLTRA
3D structure
PDB2qhx Discovery of potent pteridine reductase inhibitors to guide antiparasite drug development.
ChainB
Resolution2.61 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R17 R39 N45 N108 D181 Q186 Y194
Catalytic site (residue number reindexed from 1) R13 R35 N41 N98 D158 Q163 Y171
Enzyme Commision number 1.5.1.33: pteridine reductase.
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 NAP B R17 L18 H36 Y37 H38 R39 S40 L66 N109 A110 S111 S112 M179 V180 D181 K198 P224 L226 S227 R13 L14 H32 Y33 H34 R35 S36 L62 N99 A100 S101 S102 M156 V157 D158 K175 P201 L203 S204
BS02 FE1 B S111 F113 Y191 Y194 S101 F103 Y168 Y171 BindingDB: Ki=37nM
Gene Ontology
Molecular Function
GO:0004155 6,7-dihydropteridine reductase activity
GO:0016491 oxidoreductase activity
GO:0047040 pteridine reductase activity
Biological Process
GO:0006729 tetrahydrobiopterin biosynthetic process
GO:0031427 response to methotrexate
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:2qhx, PDBe:2qhx, PDBj:2qhx
PDBsum2qhx
PubMed18245389
UniProtQ01782|PTR1_LEIMA Pteridine reductase 1 (Gene Name=PTR1)

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