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BioLiP

Structure of PDB 1w0c Chain F

Receptor sequence
>1w0cF (length=270) Species: 5664 (Leishmania major) [Search protein sequence]
TVPVALVTGAAKRLGRSIAEGLHAEGYAVCLHYHRSAAEANALSATLNAR
RPNSAITVQADLSNVATAPSAPVTLFTRCAELVAACYTHWGRCDVLVNNA
SSFYPTPLLRNDGDREAMETATADLFGSNAIAPYFLIKAFAHRVAGTPAK
HRGTNYSIINMVDAMTNQPLLGYTIYTMAKGALEGLTRSAALELAPLQIR
VNGVGPGLSVLVDDMPPAVWEGHRSKVPLYQRDSSAAEVSDVVIFLCSSK
AKYITGTCVKVDGGYSLTRA
3D structure
PDB1w0c Inhibition of Leishmania Major Pteridine Reductase by 2,4,6-Triaminoquinazoline: Structure of the Nadph Ternary Complex
ChainF
Resolution2.6 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 D163 Y176
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 F G13 R17 L18 H36 Y37 H38 R39 S40 L66 N109 A110 S111 S112 M179 V180 D181 K198 P224 G225 L226 S227 G9 R13 L14 H32 Y33 H34 R35 S36 L62 N99 A100 S101 S102 M161 V162 D163 K180 P206 G207 L208 S209
BS02 TAQ F S111 F113 Y194 S101 F103 Y176 BindingDB: Kd=58750nM
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:1w0c, PDBe:1w0c, PDBj:1w0c
PDBsum1w0c
PubMed15388924
UniProtQ01782|PTR1_LEIMA Pteridine reductase 1 (Gene Name=PTR1)

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