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Atomistry » Calcium » PDB 1rpz-1s26 » 1rxp » |
Calcium in PDB 1rxp: Structure of Trypsin (Orthorhombic) with 1-(4-Tert- Butylcarbamoyl- Piperazine-1-Carbonyl)-3-(3-Guanidino- Propyl)-4-Oxo-Azetidine-2-Carboxylic AcidEnzymatic activity of Structure of Trypsin (Orthorhombic) with 1-(4-Tert- Butylcarbamoyl- Piperazine-1-Carbonyl)-3-(3-Guanidino- Propyl)-4-Oxo-Azetidine-2-Carboxylic Acid
All present enzymatic activity of Structure of Trypsin (Orthorhombic) with 1-(4-Tert- Butylcarbamoyl- Piperazine-1-Carbonyl)-3-(3-Guanidino- Propyl)-4-Oxo-Azetidine-2-Carboxylic Acid:
3.4.21.4; Protein crystallography data
The structure of Structure of Trypsin (Orthorhombic) with 1-(4-Tert- Butylcarbamoyl- Piperazine-1-Carbonyl)-3-(3-Guanidino- Propyl)-4-Oxo-Azetidine-2-Carboxylic Acid, PDB code: 1rxp
was solved by
G.S.Bisacchi,
B.Jacobson,
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 Structure of Trypsin (Orthorhombic) with 1-(4-Tert- Butylcarbamoyl- Piperazine-1-Carbonyl)-3-(3-Guanidino- Propyl)-4-Oxo-Azetidine-2-Carboxylic Acid
(pdb code 1rxp). 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 Structure of Trypsin (Orthorhombic) with 1-(4-Tert- Butylcarbamoyl- Piperazine-1-Carbonyl)-3-(3-Guanidino- Propyl)-4-Oxo-Azetidine-2-Carboxylic Acid, PDB code: 1rxp: Calcium binding site 1 out of 1 in 1rxpGo back to Calcium Binding Sites List in 1rxp
Calcium binding site 1 out
of 1 in the Structure of Trypsin (Orthorhombic) with 1-(4-Tert- Butylcarbamoyl- Piperazine-1-Carbonyl)-3-(3-Guanidino- Propyl)-4-Oxo-Azetidine-2-Carboxylic Acid
Mono view Stereo pair view
Reference:
J.C.Sutton,
S.A.Bolton,
M.E.Davis,
K.S.Hartl,
B.Jacobson,
A.Mathur,
M.L.Ogletree,
W.A.Slusarchyk,
R.Zahler,
S.M.Seiler,
G.S.Bisacchi.
Solid-Phase Synthesis and Sar of 4-Carboxy-2-Azetidinone Mechanism-Based Tryptase Inhibitors Bioorg.Med.Chem.Lett. V. 14 2233 2004.
Page generated: Sat Dec 12 03:18:11 2020
ISSN: ISSN 0960-894X PubMed: 15081015 DOI: 10.1016/J.BMCL.2004.02.012 |
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