BioLiP

Receptor Information

>2bfp Chain C (length=256) Species: 5664 (Leishmania major) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]

TVPVALVTGAAKRLGRSIAEGLHAEGYAVCLHYHRSAAEANALSATLNAR
RPNSAITVQADLSNVATAPAPVTLFTRCAELVAACYTHWGRCDVLVNNAS
SFYPTPLLRREAMETATADLFGSNAIAPYFLIKAFAHRVAGTPAKHRGTN
YSIINMVDAMTNQPLLGYTIYTMAKGALEGLTRSAALELAPLQIRVNGVG
PGLSVLVGHRSKVPLYQRDSSAAEVSDVVIFLCSSKAKYITGTCVKVDGG
YSLTRA

Ligand ID

NAP

InChI

InChI=1S/C21H28N7O17P3/c22-17-12-19(25-7-24-17)28(8-26-12)21-16(44-46(33,34)35)14(30)11(43-21)6-41-48(38,39)45-47(36,37)40-5-10-13(29)15(31)20(42-10)27-3-1-2-9(4-27)18(23)32/h1-4,7-8,10-11,13-16,20-21,29-31H,5-6H2,(H7-,22,23,24,25,32,33,34,35,36,37,38,39)/t10-,11-,13-,14-,15-,16-,20-,21-/m1/s1

InChIKey

XJLXINKUBYWONI-NNYOXOHSSA-N

SMILES

Software	SMILES
OpenEye OEToolkits 1.5.0	c1cc(c[n+](c1)C2C(C(C(O2)COP(=O)([O-])OP(=O)(O)OCC3C(C(C(O3)n4cnc5c4ncnc5N)OP(=O)(O)O)O)O)O)C(=O)N
CACTVS 3.341	NC(=O)c1ccc[n+](c1)[CH]2O[CH](CO[P]([O-])(=O)O[P](O)(=O)OC[CH]3O[CH]([CH](O[P](O)(O)=O)[CH]3O)n4cnc5c(N)ncnc45)[CH](O)[CH]2O
CACTVS 3.341	NC(=O)c1ccc[n+](c1)[C@@H]2O[C@H](CO[P]([O-])(=O)O[P@@](O)(=O)OC[C@H]3O[C@H]([C@H](O[P](O)(O)=O)[C@@H]3O)n4cnc5c(N)ncnc45)[C@@H](O)[C@H]2O
OpenEye OEToolkits 1.5.0	c1cc(c[n+](c1)[C@H]2[C@@H]([C@@H]([C@H](O2)CO[P@@](=O)([O-])O[P@](=O)(O)OC[C@@H]3[C@H]([C@H]([C@@H](O3)n4cnc5c4ncnc5N)OP(=O)(O)O)O)O)O)C(=O)N

Formula

C21 H28 N7 O17 P3

Name

NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE;
2'-MONOPHOSPHOADENOSINE 5'-DIPHOSPHORIBOSE

PDB chain

2bfp Chain C Residue 1289 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	2bfp Structures of Leishmania Major Pteridine Reductase Complexes Reveal the Active Site Features Important for Ligand Binding and to Guide Inhibitor Design
Resolution	2.55 Å
Binding residue (original residue number in PDB)	R17 L18 H36 Y37 H38 R39 S40 D65 L66 N109 A110 S111 M179 K198 P224 L226 S227
Binding residue (residue number reindexed from 1)	R13 L14 H32 Y33 H34 R35 S36 D61 L62 N98 A99 S100 M156 K175 P201 L203 S204
Annotation score	4

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.

	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

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

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Structure of PDB 2bfp Chain C Binding Site BS01