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Protein
Submitted name:

Pteridine reductase

Gene

PTR1

Organism
Trypanosoma brucei brucei
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei14 – 141SubstrateCombined sources
Active sitei161 – 1611Proton donor/acceptorCombined sources
Active sitei174 – 1741Proton donor/acceptorCombined sources
Binding sitei174 – 1741NADPCombined sources
Binding sitei178 – 1781NADPCombined sources

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 152NADPCombined sources
Nucleotide bindingi35 – 373NADPCombined sources
Nucleotide bindingi62 – 643NADPCombined sources
Nucleotide bindingi93 – 953NADPCombined sources
Nucleotide bindingi204 – 2085NADPCombined sources

GO - Molecular functioni

  1. nucleotide binding Source: UniProtKB-KW
  2. oxidoreductase activity Source: InterPro
Complete GO annotation...

Keywords - Ligandi

NADPCombined sources, Nucleotide-bindingCombined sources

Names & Taxonomyi

Protein namesi
Submitted name:
Pteridine reductaseImported
Gene namesi
Name:PTR1Imported
OrganismiTrypanosoma brucei bruceiImported
Taxonomic identifieri5702 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosoma

Interactioni

Protein-protein interaction databases

STRINGi5691.Tb927.8.2210.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C7VX-ray2.20A/B/C/D1-268[»]
2VZ0X-ray1.90A/B/C/D1-268[»]
2WD7X-ray1.90A/B/C/D1-268[»]
2WD8X-ray2.10A/B/C/D1-268[»]
2X9GX-ray1.10A/B/C/D1-268[»]
2X9NX-ray1.15A/B/C/D1-268[»]
2X9VX-ray1.30A/B/C/D1-268[»]
2YHUX-ray2.01A/B/C/D1-268[»]
3BMCX-ray2.60A/B/C/D1-268[»]
3BMNX-ray1.98A/B/C/D1-268[»]
3BMOX-ray1.60A/B/C/D1-268[»]
3BMQX-ray1.70A/B/C/D1-268[»]
3GN1X-ray2.00A/B/C/D1-268[»]
3GN2X-ray1.60A/B/C/D1-268[»]
3MCVX-ray1.70A/B/C/D1-268[»]
ProteinModelPortaliO76290.
SMRiO76290. Positions 2-268.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO76290.

Family & Domainsi

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR014058. Pteridine_reductase.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
TIGRFAMsiTIGR02685. pter_reduc_Leis. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O76290-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEAPAAVVTG AAKRIGRAIA VKLHQTGYRV VIHYHNSAEA AVSLADELNK
60 70 80 90 100
ERSNTAVVCQ ADLTNSNVLP ASCEEIINSC FRAFGRCDVL VNNASAFYPT
110 120 130 140 150
PLVQGDHEDN SNGKTVETQV AELIGTNAIA PFLLTMSFAQ RQKGTNPNCT
160 170 180 190 200
SSNLSIVNLC DAMVDQPCMA FSLYNMGKHA LVGLTQSAAL ELAPYGIRVN
210 220 230 240 250
GVAPGVSLLP VAMGEEEKDK WRRKVPLGRR EASAEQIADA VIFLVSGSAQ
260
YITGSIIKVD GGLSLVHA
Length:268
Mass (Da):28,470
Last modified:November 1, 1998 - v1
Checksum:i346C8257BDC9DD3D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF049903 mRNA. Translation: AAC23562.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF049903 mRNA. Translation: AAC23562.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C7VX-ray2.20A/B/C/D1-268[»]
2VZ0X-ray1.90A/B/C/D1-268[»]
2WD7X-ray1.90A/B/C/D1-268[»]
2WD8X-ray2.10A/B/C/D1-268[»]
2X9GX-ray1.10A/B/C/D1-268[»]
2X9NX-ray1.15A/B/C/D1-268[»]
2X9VX-ray1.30A/B/C/D1-268[»]
2YHUX-ray2.01A/B/C/D1-268[»]
3BMCX-ray2.60A/B/C/D1-268[»]
3BMNX-ray1.98A/B/C/D1-268[»]
3BMOX-ray1.60A/B/C/D1-268[»]
3BMQX-ray1.70A/B/C/D1-268[»]
3GN1X-ray2.00A/B/C/D1-268[»]
3GN2X-ray1.60A/B/C/D1-268[»]
3MCVX-ray1.70A/B/C/D1-268[»]
ProteinModelPortaliO76290.
SMRiO76290. Positions 2-268.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi5691.Tb927.8.2210.

Chemistry

BindingDBiO76290.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiO76290.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR002198. DH_sc/Rdtase_SDR.
IPR002347. Glc/ribitol_DH.
IPR016040. NAD(P)-bd_dom.
IPR014058. Pteridine_reductase.
IPR020904. Sc_DH/Rdtase_CS.
[Graphical view]
PRINTSiPR00081. GDHRDH.
PR00080. SDRFAMILY.
TIGRFAMsiTIGR02685. pter_reduc_Leis. 1 hit.
PROSITEiPS00061. ADH_SHORT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Detke S.
    Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Structure and reactivity of Trypanosoma brucei pteridine reductase: inhibition by the archetypal antifolate methotrexate."
    Dawson A., Gibellini F., Sienkiewicz N., Tulloch L.B., Fyfe P.K., McLuskey K., Fairlamb A.H., Hunter W.N.
    Mol. Microbiol. 61:1457-1468(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH NADP, ACTIVE SITE.
  3. "One scaffold, three binding modes: novel and selective pteridine reductase 1 inhibitors derived from fragment hits discovered by virtual screening."
    Mpamhanga C.P., Spinks D., Tulloch L.B., Shanks E.J., Robinson D.A., Collie I.T., Fairlamb A.H., Wyatt P.G., Frearson J.A., Hunter W.N., Gilbert I.H., Brenk R.
    J. Med. Chem. 52:4454-4465(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH NADP.
  4. "High-resolution structures of Trypanosoma brucei pteridine reductase ligand complexes inform on the placement of new molecular entities in the active site of a potential drug target."
    Dawson A., Tulloch L.B., Barrack K.L., Hunter W.N.
    Acta Crystallogr. D 66:1334-1340(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.10 ANGSTROMS) IN COMPLEX WITH NADP.
  5. "Development and validation of a cytochrome c-coupled assay for pteridine reductase 1 and dihydrofolate reductase."
    Shanks E.J., Ong H.B., Robinson D.A., Thompson S., Sienkiewicz N., Fairlamb A.H., Frearson J.A.
    Anal. Biochem. 396:194-203(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH NADP.
  6. "Structure-based design of pteridine reductase inhibitors targeting African sleeping sickness and the leishmaniases."
    Tulloch L.B., Martini V.P., Iulek J., Huggan J.K., Lee J.H., Gibson C.L., Smith T.K., Suckling C.J., Hunter W.N.
    J. Med. Chem. 53:221-229(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH NADP.
  7. "Structural Studies of Thiadiazole Derivatives that Inhibit Trypanosoma Brucei Growth."
    Nerini E., Dawson A., Hannaert V., Michels P.A., Hunter W.N., Costi M.P.
    Submitted (MAY-2011) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH NADP.

Entry informationi

Entry nameiO76290_TRYBB
AccessioniPrimary (citable) accession number: O76290
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1998
Last sequence update: November 1, 1998
Last modified: January 7, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.