Structure of PDB 1e92 Chain C

Receptor sequence
>1e92C (length=257) Species: 5664 (Leishmania major) [Search protein sequence]
VPVALVTGAAKRLGRSIAEGLHAEGYAVCLHYHRSAAEANALSATLNARR
PNSAITVQADLSNVATAPAPVTLFTRCAELVAACYTHWGRCDVLVNNASS
FYPTPLLRNDREAMETATADLFGSNAIAPYFLIKAFAHRVAGTPAKHRGT
NYSIINMVDAMTNQPLLGYTIYTMAKGALEGLTRSAALELAPLQIRVNGV
GPGLSVLVGHRSKVPLYQRDSSAAEVSDVVIFLCSSKAKYITGTCVKVDG
GYSLTRA
3D structure
PDB1e92 Pteridine Reductase Mechanism Correlates Pterin Metabolism with Drug Resistance in Trypanosomatid Parasites
ChainC
Resolution2.2 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 D181 Y194
Catalytic site (residue number reindexed from 1) R12 D159 Y172
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 C R17 L18 H36 Y37 H38 R39 S40 D65 L66 N109 A110 S111 S112 M179 D181 K198 P224 G225 L226 S227 R12 L13 H31 Y32 H33 R34 S35 D60 L61 N97 A98 S99 S100 M157 D159 K176 P202 G203 L204 S205
BS02 HBI C S111 F113 Y194 L226 S99 F101 Y172 L204
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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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:1e92, PDBe:1e92, PDBj:1e92
PDBsum1e92
PubMed11373620
UniProtQ01782|PTR1_LEIMA Pteridine reductase 1 (Gene Name=PTR1)

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