Structure of PDB 2bfp Chain A

Receptor sequence
>2bfpA (length=267) Species: 5664 (Leishmania major) [Search protein sequence]
VPVALVTGAAKRLGRSIAEGLHAEGYAVCLHYHRSAAEANALSATLNARR
PNSAITVQADLSNVATAPAPVTLFTRCAELVAACYTHWGRCDVLVNNASS
FYPTPLLRNGDREAMETATADLFGSNAIAPYFLIKAFAHRVAGTPAKHRG
TNYSIINMVDAMTNQPLLGYTIYTMAKGALEGLTRSAALELAPLQIRVNG
VGPGLSVLVDDMPPAVWEGHRSKVPLYQRDSSAAEVSDVVIFLCSSKAKY
ITGTCVKVDGGYSLTRA
3D structure
PDB2bfp Structures of Leishmania Major Pteridine Reductase Complexes Reveal the Active Site Features Important for Ligand Binding and to Guide Inhibitor Design
ChainA
Resolution2.55 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) R17 D181 Y194
Catalytic site (residue number reindexed from 1) R12 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 NAP A R17 L18 Y37 H38 R39 S40 L66 N109 A110 S111 S112 M179 K198 P224 L226 S227 R12 L13 Y32 H33 R34 S35 L61 N97 A98 S99 S100 M158 K177 P203 L205 S206
BS02 H4B A S111 F113 Y194 L226 S99 F101 Y173 L205
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2bfp, PDBe:2bfp, PDBj:2bfp
PDBsum2bfp
PubMed16055151
UniProtQ01782|PTR1_LEIMA Pteridine reductase 1 (Gene Name=PTR1)

[Back to BioLiP]