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Atomistry » Calcium » PDB 5mop-5n2x » 5mos | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 5mop-5n2x » 5mos » |
Calcium in PDB 5mos: Joint X-Ray/Neutron Structure of Cationic Trypsin in Complex with N- AmidinopiperidineEnzymatic activity of Joint X-Ray/Neutron Structure of Cationic Trypsin in Complex with N- Amidinopiperidine
All present enzymatic activity of Joint X-Ray/Neutron Structure of Cationic Trypsin in Complex with N- Amidinopiperidine:
3.4.21.4; Protein crystallography data
The structure of Joint X-Ray/Neutron Structure of Cationic Trypsin in Complex with N- Amidinopiperidine, PDB code: 5mos
was solved by
J.Schiebel,
T.E.Schrader,
A.Ostermann,
A.Heine,
G.Klebe,
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 Joint X-Ray/Neutron Structure of Cationic Trypsin in Complex with N- Amidinopiperidine
(pdb code 5mos). 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 Joint X-Ray/Neutron Structure of Cationic Trypsin in Complex with N- Amidinopiperidine, PDB code: 5mos: Calcium binding site 1 out of 1 in 5mosGo back to Calcium Binding Sites List in 5mos
Calcium binding site 1 out
of 1 in the Joint X-Ray/Neutron Structure of Cationic Trypsin in Complex with N- Amidinopiperidine
Mono view Stereo pair view
Reference:
J.Schiebel,
R.Gaspari,
T.Wulsdorf,
K.Ngo,
C.Sohn,
T.E.Schrader,
A.Cavalli,
A.Ostermann,
A.Heine,
G.Klebe.
Intriguing Role of Water in Protein-Ligand Binding Studied By Neutron Crystallography on Trypsin Complexes. Nat Commun V. 9 3559 2018.
Page generated: Mon Jul 15 08:34:26 2024
ISSN: ESSN 2041-1723 PubMed: 30177695 DOI: 10.1038/S41467-018-05769-2 |
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