Structure of PDB 2bfm Chain A

Receptor sequence
>2bfmA (length=266) Species: 5664 (Leishmania major) [Search protein sequence]
VPVALVTGAAKRLGRSIAEGLHAEGYAVCLHYHRSAAEANALSATLNARR
PNSAITVQADLSNVATAPAPVTLFTRCAELVAACYTHWGRCDVLVNNASS
FYPTPLLRGDREAMETATADLFGSNAIAPYFLIKAFAHRVAGTPAKHRGT
NYSIINMVDAMTNQPLLGYTIYTMAKGALEGLTRSAALELAPLQIRVNGV
GPGLSVLVDDMPPAVWEGHRSKVPLYQRDSSAAEVSDVVIFLCSSKAKYI
TGTCVKVDGGYSLTRA
3D structure
PDB2bfm Structures of Leishmania Major Pteridine Reductase Complexes Reveal the Active Site Features Important for Ligand Binding and to Guide Inhibitor Design
ChainA
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) 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 NDP A R17 L18 Y37 H38 R39 S40 L66 N109 A110 S111 M179 V180 D181 K198 P224 L226 S227 R12 L13 Y32 H33 R34 S35 L61 N97 A98 S99 M157 V158 D159 K176 P202 L204 S205
BS02 TOP A F113 L188 Y194 L226 H241 F101 L166 Y172 L204 H219
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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Cellular Component
External links
PDB RCSB:2bfm, PDBe:2bfm, PDBj:2bfm
PDBsum2bfm
PubMed16055151
UniProtQ01782|PTR1_LEIMA Pteridine reductase 1 (Gene Name=PTR1)

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