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Atomistry » Calcium » PDB 2xqg-2y6h » 2xtt | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 2xqg-2y6h » 2xtt » |
Calcium in PDB 2xtt: Bovine Trypsin in Complex with Evolutionary Enhanced Schistocerca Gregaria Protease Inhibitor 1 (Sgpi-1-P02)Enzymatic activity of Bovine Trypsin in Complex with Evolutionary Enhanced Schistocerca Gregaria Protease Inhibitor 1 (Sgpi-1-P02)
All present enzymatic activity of Bovine Trypsin in Complex with Evolutionary Enhanced Schistocerca Gregaria Protease Inhibitor 1 (Sgpi-1-P02):
3.4.21.4; Protein crystallography data
The structure of Bovine Trypsin in Complex with Evolutionary Enhanced Schistocerca Gregaria Protease Inhibitor 1 (Sgpi-1-P02), PDB code: 2xtt
was solved by
W.Y.Wahlgren,
G.Pal,
J.Kardos,
P.Porrogi,
B.Szenthe,
A.Patthy,
L.Graf,
G.Katona,
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 Bovine Trypsin in Complex with Evolutionary Enhanced Schistocerca Gregaria Protease Inhibitor 1 (Sgpi-1-P02)
(pdb code 2xtt). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Bovine Trypsin in Complex with Evolutionary Enhanced Schistocerca Gregaria Protease Inhibitor 1 (Sgpi-1-P02), PDB code: 2xtt: Calcium binding site 1 out of 1 in 2xttGo back to Calcium Binding Sites List in 2xtt
Calcium binding site 1 out
of 1 in the Bovine Trypsin in Complex with Evolutionary Enhanced Schistocerca Gregaria Protease Inhibitor 1 (Sgpi-1-P02)
Mono view Stereo pair view
Reference:
W.Y.Wahlgren,
G.Pal,
J.Kardos,
P.Porrogi,
B.Szenthe,
A.Patthy,
L.Graf,
G.Katona.
The Catalytic Aspartate Is Protonated in the Michaelis Complex Formed Between Trypsin and An in Vitro Evolved Substrate-Like Inhibitor: A Refined Mechanism of Serine Protease Action. J.Biol.Chem. V. 286 3587 2011.
Page generated: Fri Jul 12 19:16:14 2024
ISSN: ESSN 1083-351X PubMed: 21097875 DOI: 10.1074/JBC.M110.161604 |
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