Structure of PDB 2bfa Chain D

Receptor sequence
>2bfaD (length=255) Species: 5664 (Leishmania major) [Search protein sequence]
VPVALVTGAAKRLGRSIAEGLHAEGYAVCLHYHRSAAEANALSATLNARR
PNSAITVQADLSNVATAPAPVTLFTRCAELVAACYTHWGRCDVLVNNASS
FYPTPLLRDREAMETATADLFGSNAIAPYFLIKAFAHRVAGTPAKHRGTN
YSIINMVDAMTNQPLLGYTIYTMAKGALEGLTRSAALELAPLQIRVNGVG
PGLSVLVHRSKVPLYQRDSSAAEVSDVVIFLCSSKAKYITGTCVKVDGGY
SLTRA
3D structure
PDB2bfa Structures of Leishmania Major Pteridine Reductase Complexes Reveal the Active Site Features Important for Ligand Binding and to Guide Inhibitor Design
ChainD
Resolution2.7 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 D158 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 NDP D R17 L18 H36 H38 R39 S40 D65 L66 N109 S111 S112 M179 V180 D181 K198 P224 G225 L226 S227 R12 L13 H31 H33 R34 S35 D60 L61 N97 S99 S100 M156 V157 D158 K175 P201 G202 L203 S204
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:2bfa, PDBe:2bfa, PDBj:2bfa
PDBsum2bfa
PubMed16055151
UniProtQ01782|PTR1_LEIMA Pteridine reductase 1 (Gene Name=PTR1)

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