Structure of PDB 1e7w Chain A

Receptor sequence
>1e7wA (length=267) Species: 5664 (Leishmania major) [Search protein sequence]
TVPVALVTGAAKRLGRSIAEGLHAEGYAVCLHYHRSAAEANALSATLNAR
RPNSAITVQADLSNVATAPVSSAPVTLFTRCAELVAACYTHWGRCDVLVN
NASSFYPTPLLREAMETATADLFGSNAIAPYFLIKAFAHRVAGTPAKHRG
TNYSIINMVDAMTNQPLLGYTIYTMAKGALEGLTRSAALELAPLQIRVNG
VGPGLSVLVDDMPPAVWEGHRSKVPLYQRDSSAAEVSDVVIFLCSSKAKY
ITGTCVKVDGGYSLTRA
3D structure
PDB1e7w Pteridine Reductase Mechanism Correlates Pterin Metabolism with Drug Resistance in Trypanosomatid Parasites.
ChainA
Resolution1.75 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) R13 D160 Y173
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 NDP A R17 L18 H36 Y37 H38 R39 S40 L66 N109 A110 S111 M179 D181 K198 P224 L226 S227 R13 L14 H32 Y33 H34 R35 S36 L62 N101 A102 S103 M158 D160 K177 P203 L205 S206
BS02 MTX A S111 F113 L188 Y191 Y194 D232 M233 S103 F105 L167 Y170 Y173 D211 M212 BindingDB: Ki=180nM
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:1e7w, PDBe:1e7w, PDBj:1e7w
PDBsum1e7w
PubMed11373620
UniProtQ01782|PTR1_LEIMA Pteridine reductase 1 (Gene Name=PTR1)

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