Structure of PDB 2bfp Chain B

Receptor sequence

>2bfpB (length=266) Species: 5664 (Leishmania major)

TVPVALVTGAAKRLGRSIAEGLHAEGYAVCLHYHRSAAEANALSATLNAR
RPNSAITVQADLSNVATAPAPVTLFTRCAELVAACYTHWGRCDVLVNNAS
SFYPTPLLGDREAMETATADLFGSNAIAPYFLIKAFAHRVAGTPAKHRGT
NYSIINMVDAMTNQPLLGYTIYTMAKGALEGLTRSAALELAPLQIRVNGV
GPGLSVLVDDMPPAVWEGHRSKVPLYQRDSSAAEVSDVVIFLCSSKAKYI
TGTCVKVDGGYSLTRA

3D structure

• PDB: 2bfp Structures of Leishmania Major Pteridine Reductase Complexes Reveal the Active Site Features Important for Ligand Binding and to Guide Inhibitor Design
• Chain: B
• Resolution: 2.55 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): R17 D181 Y194
• Catalytic site (residue number reindexed from 1): R13 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	NAP	B	R17 L18 H36 Y37 H38 R39 S40 L66 N109 A110 S111 S112 M179 D181 K198 P224 G225 L226 S227	R13 L14 H32 Y33 H34 R35 S36 L62 N98 A99 S100 S101 M157 D159 K176 P202 G203 L204 S205
BS02	H4B	B	S111 F113 Y194 L226 L229	S100 F102 Y172 L204 L207

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

External links

• PDB: RCSB:2bfp, PDBe:2bfp, PDBj:2bfp
• PDBsum: 2bfp
• PubMed: 16055151
• UniProt: Q01782|PTR1_LEIMA Pteridine reductase 1 (Gene Name=PTR1)