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Atomistry » Zinc » PDB 3ptk-3q7c » 3pz4 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 3ptk-3q7c » 3pz4 » |
Zinc in PDB 3pz4: Crystal Structure of Ftase(Alpha-Subunit; Beta-Subunit Delta C10) in Complex with BMS3 and Lipid Substrate FppEnzymatic activity of Crystal Structure of Ftase(Alpha-Subunit; Beta-Subunit Delta C10) in Complex with BMS3 and Lipid Substrate Fpp
All present enzymatic activity of Crystal Structure of Ftase(Alpha-Subunit; Beta-Subunit Delta C10) in Complex with BMS3 and Lipid Substrate Fpp:
2.5.1.58; 2.5.1.59; Protein crystallography data
The structure of Crystal Structure of Ftase(Alpha-Subunit; Beta-Subunit Delta C10) in Complex with BMS3 and Lipid Substrate Fpp, PDB code: 3pz4
was solved by
Z.Guo,
R.S.Bon,
E.A.Stigter,
H.Waldmann,
K.Alexandrov,
W.Blankenfeldt,
R.S.Goody,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Ftase(Alpha-Subunit; Beta-Subunit Delta C10) in Complex with BMS3 and Lipid Substrate Fpp
(pdb code 3pz4). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Ftase(Alpha-Subunit; Beta-Subunit Delta C10) in Complex with BMS3 and Lipid Substrate Fpp, PDB code: 3pz4: Zinc binding site 1 out of 1 in 3pz4Go back to![]() ![]()
Zinc binding site 1 out
of 1 in the Crystal Structure of Ftase(Alpha-Subunit; Beta-Subunit Delta C10) in Complex with BMS3 and Lipid Substrate Fpp
![]() Mono view ![]() Stereo pair view
Reference:
R.S.Bon,
Z.Guo,
E.A.Stigter,
S.Wetzel,
S.Menninger,
A.Wolf,
A.Choidas,
K.Alexandrov,
W.Blankenfeldt,
R.S.Goody,
H.Waldmann.
Structure-Guided Development of Selective Rabggtase Inhibitors. Angew.Chem.Int.Ed.Engl. V. 50 4957 2011.
Page generated: Wed Dec 16 04:44:16 2020
ISSN: ISSN 1433-7851 PubMed: 21520375 DOI: 10.1002/ANIE.201101210 |
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