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Atomistry » Calcium » PDB 7p9t-7po7 » 7ph1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 7p9t-7po7 » 7ph1 » |
Calcium in PDB 7ph1: Trypsin in Complex with Bpti Mutant (2S)-2-Amino-4-Monofluorobutanoic AcidEnzymatic activity of Trypsin in Complex with Bpti Mutant (2S)-2-Amino-4-Monofluorobutanoic Acid
All present enzymatic activity of Trypsin in Complex with Bpti Mutant (2S)-2-Amino-4-Monofluorobutanoic Acid:
3.4.21.4; Protein crystallography data
The structure of Trypsin in Complex with Bpti Mutant (2S)-2-Amino-4-Monofluorobutanoic Acid, PDB code: 7ph1
was solved by
N.Dimos,
J.Leppkes,
B.Koksch,
B.Loll,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 7ph1:
The structure of Trypsin in Complex with Bpti Mutant (2S)-2-Amino-4-Monofluorobutanoic Acid also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Trypsin in Complex with Bpti Mutant (2S)-2-Amino-4-Monofluorobutanoic Acid
(pdb code 7ph1). 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 Trypsin in Complex with Bpti Mutant (2S)-2-Amino-4-Monofluorobutanoic Acid, PDB code: 7ph1: Calcium binding site 1 out of 1 in 7ph1Go back to![]() ![]()
Calcium binding site 1 out
of 1 in the Trypsin in Complex with Bpti Mutant (2S)-2-Amino-4-Monofluorobutanoic Acid
![]() Mono view ![]() Stereo pair view
Reference:
L.Wehrhan,
J.Leppkes,
N.Dimos,
B.Loll,
B.Koksch,
B.G.Keller.
Water Network in the Binding Pocket of Fluorinated Bpti-Trypsin Complexes─Insights From Simulation and Experiment. J.Phys.Chem.B V. 126 9985 2022.
Page generated: Thu Jul 10 00:08:53 2025
ISSN: ISSN 1089-5647 PubMed: 36409613 DOI: 10.1021/ACS.JPCB.2C05496 |
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