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Atomistry » Calcium » PDB 1tkj-1ttx » 1trq » |
Calcium in PDB 1trq: X-Ray Crystallographic and Calorimeric Studies of the Effects of the Mutation Trp 59 Tyr in Ribonuclease T1Enzymatic activity of X-Ray Crystallographic and Calorimeric Studies of the Effects of the Mutation Trp 59 Tyr in Ribonuclease T1
All present enzymatic activity of X-Ray Crystallographic and Calorimeric Studies of the Effects of the Mutation Trp 59 Tyr in Ribonuclease T1:
3.1.27.3; Protein crystallography data
The structure of X-Ray Crystallographic and Calorimeric Studies of the Effects of the Mutation Trp 59 Tyr in Ribonuclease T1, PDB code: 1trq
was solved by
W.-D.Schubert,
W.Saenger,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Calcium Binding Sites:
The binding sites of Calcium atom in the X-Ray Crystallographic and Calorimeric Studies of the Effects of the Mutation Trp 59 Tyr in Ribonuclease T1
(pdb code 1trq). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the X-Ray Crystallographic and Calorimeric Studies of the Effects of the Mutation Trp 59 Tyr in Ribonuclease T1, PDB code: 1trq: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 1trqGo back to Calcium Binding Sites List in 1trq
Calcium binding site 1 out
of 2 in the X-Ray Crystallographic and Calorimeric Studies of the Effects of the Mutation Trp 59 Tyr in Ribonuclease T1
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 1trqGo back to Calcium Binding Sites List in 1trq
Calcium binding site 2 out
of 2 in the X-Ray Crystallographic and Calorimeric Studies of the Effects of the Mutation Trp 59 Tyr in Ribonuclease T1
Mono view Stereo pair view
Reference:
W.D.Schubert,
G.Schluckebier,
J.Backmann,
J.Granzin,
C.Kisker,
H.W.Choe,
U.Hahn,
W.Pfeil,
W.Saenger.
X-Ray Crystallographic and Calorimetric Studies of the Effects of the Mutation TRP59-->Tyr in Ribonuclease T1. Eur.J.Biochem. V. 220 527 1994.
Page generated: Thu Jul 11 23:11:53 2024
ISSN: ISSN 0014-2956 PubMed: 8125111 DOI: 10.1111/J.1432-1033.1994.TB18652.X |
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