Structure of PDB 2bfp Chain C

Receptor sequence
>2bfpC (length=256) Species: 5664 (Leishmania major) [Search protein sequence]
TVPVALVTGAAKRLGRSIAEGLHAEGYAVCLHYHRSAAEANALSATLNAR
RPNSAITVQADLSNVATAPAPVTLFTRCAELVAACYTHWGRCDVLVNNAS
SFYPTPLLRREAMETATADLFGSNAIAPYFLIKAFAHRVAGTPAKHRGTN
YSIINMVDAMTNQPLLGYTIYTMAKGALEGLTRSAALELAPLQIRVNGVG
PGLSVLVGHRSKVPLYQRDSSAAEVSDVVIFLCSSKAKYITGTCVKVDGG
YSLTRA
3D structure
PDB2bfp Structures of Leishmania Major Pteridine Reductase Complexes Reveal the Active Site Features Important for Ligand Binding and to Guide Inhibitor Design
ChainC
Resolution2.55 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 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 NAP C R17 L18 H36 Y37 H38 R39 S40 D65 L66 N109 A110 S111 M179 K198 P224 L226 S227 R13 L14 H32 Y33 H34 R35 S36 D61 L62 N98 A99 S100 M156 K175 P201 L203 S204
BS02 H4B C S111 F113 Y194 L226 S100 F102 Y171 L203
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:2bfp, PDBe:2bfp, PDBj:2bfp
PDBsum2bfp
PubMed16055151
UniProtQ01782|PTR1_LEIMA Pteridine reductase 1 (Gene Name=PTR1)

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