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Q95WL3

- Q95WL3_TRYCR

UniProt

Q95WL3 - Q95WL3_TRYCR

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Protein
Submitted name: Farnesyl pyrophosphate synthase
Gene
N/A
Organism
Trypanosoma cruzi
Status
Unreviewed - Annotation score: 2 out of 5 - Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei91 – 911Sulfate 4
Metal bindingi176 – 1761SodiumImported
Metal bindingi190 – 1901SodiumImported
Metal bindingi191 – 1911Sodium; via amide nitrogenImported

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. transferase activity Source: UniProtKB-KW

GO - Biological processi

  1. isoprenoid biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

TransferaseUniRule annotation

Keywords - Biological processi

Isoprene biosynthesisUniRule annotation

Keywords - Ligandi

Metal-bindingImported, SodiumImported

Names & Taxonomyi

Protein namesi
Submitted name:
Farnesyl pyrophosphate synthaseImported
OrganismiTrypanosoma cruziImported
Taxonomic identifieri5693 [NCBI]
Taxonomic lineageiEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeTrypanosomaSchizotrypanum

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IBAX-ray2.40A1-362[»]
3ICKX-ray2.40A1-362[»]
3ICMX-ray2.20A1-362[»]
3ICNX-ray2.40A1-362[»]
3ICZX-ray2.15A1-362[»]
4DWBX-ray2.10A1-362[»]
4DWGX-ray2.01A1-362[»]
4DXJX-ray2.35A/B/C1-362[»]
4DZWX-ray3.05A1-362[»]
4E1EX-ray2.65A2-362[»]
ProteinModelPortaliQ95WL3.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni48 – 514Sulfate 4 binding

Sequence similaritiesi

Belongs to the FPP/GGPP synthase family.UniRule annotation

Family and domain databases

Gene3Di1.10.600.10. 1 hit.
InterProiIPR000092. Polyprenyl_synt.
IPR008949. Terpenoid_synth.
[Graphical view]
PfamiPF00348. polyprenyl_synt. 1 hit.
[Graphical view]
SUPFAMiSSF48576. SSF48576. 1 hit.
PROSITEiPS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

Q95WL3-1 [UniParc]FASTAAdd to Basket

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MASMERFLSV YDEVQAFLLD QLQSKYEIDP NRARYLRIMM DTTCLGGKYF    50
RGMTVVNVAE GFLAVTQHDE ATKERILHDA CVGGWMIEFL QAHYLVEDDI 100
MDGSVMRRGK PCWYRFPGVT TQCAINDGII LKSWTQIMAW HYFADRPFLK 150
DLLCLFQKVD YATAVGQMYD VTSMCDSNKL DPEVAQPMTT DFAEFTPAIY 200
KRIVKYKTTF YTYLLPLVMG LFVSEAAASV EMNLVERVAH LIGEYFQVQD 250
DVMDCFTPPE QLGKVGTDIE DAKCSWLAVT FLGKANAAQV AEFKANYGDK 300
DPAKVAVVKR LYSEANLQAD FAAYEAEVVR EVESLIEQLK VKSPTFAESV 350
AVVWEKTHKR KK 362
Length:362
Mass (Da):41,180
Last modified:December 1, 2001 - v1
Checksum:iCF2CB54BA03B3DB0
GO

Non-terminal residue

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei362 – 3621Imported

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF312690 Genomic DNA. Translation: AAK71861.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF312690 Genomic DNA. Translation: AAK71861.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3IBA X-ray 2.40 A 1-362 [» ]
3ICK X-ray 2.40 A 1-362 [» ]
3ICM X-ray 2.20 A 1-362 [» ]
3ICN X-ray 2.40 A 1-362 [» ]
3ICZ X-ray 2.15 A 1-362 [» ]
4DWB X-ray 2.10 A 1-362 [» ]
4DWG X-ray 2.01 A 1-362 [» ]
4DXJ X-ray 2.35 A/B/C 1-362 [» ]
4DZW X-ray 3.05 A 1-362 [» ]
4E1E X-ray 2.65 A 2-362 [» ]
ProteinModelPortali Q95WL3.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

Gene3Di 1.10.600.10. 1 hit.
InterProi IPR000092. Polyprenyl_synt.
IPR008949. Terpenoid_synth.
[Graphical view ]
Pfami PF00348. polyprenyl_synt. 1 hit.
[Graphical view ]
SUPFAMi SSF48576. SSF48576. 1 hit.
PROSITEi PS00723. POLYPRENYL_SYNTHASE_1. 1 hit.
PS00444. POLYPRENYL_SYNTHASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Bisphosphonates are potent inhibitors of Trypanosoma cruzi farnesyl pyrophosphate synthase."
    Montalvetti A., Bailey B.N., Martin M.B., Severin G.W., Oldfield E., Docampo R.
    J. Biol. Chem. 276:33930-33937(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. "Binding of nitrogen-containing bisphosphonates (N-BPs) to the Trypanosoma cruzi farnesyl diphosphate synthase homodimer."
    Huang C.H., Gabelli S.B., Oldfield E., Amzel L.M.
    Proteins 78:888-899(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
  3. "Design, synthesis, calorimetry, and crystallographic analysis of 2-alkylaminoethyl-1,1-bisphosphonates as inhibitors of Trypanosoma cruzi farnesyl diphosphate synthase."
    Aripirala S., Szajnman S.H., Jakoncic J., Rodriguez J.B., Docampo R., Gabelli S.B., Amzel L.M.
    J. Med. Chem. 55:6445-6454(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH SODIUM.

Entry informationi

Entry nameiQ95WL3_TRYCR
AccessioniPrimary (citable) accession number: Q95WL3
Entry historyi
Integrated into UniProtKB/TrEMBL: December 1, 2001
Last sequence update: December 1, 2001
Last modified: September 3, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported

External Data

Dasty 3

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