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Atomistry » Zinc » PDB 1k6y-1kk0 » 1kap | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 1k6y-1kk0 » 1kap » |
Zinc in PDB 1kap: Three-Dimensional Structure of the Alkaline Protease of Pseudomonas Aeruginosa: A Two-Domain Protein with A Calcium Binding Parallel Beta Roll MotifProtein crystallography data
The structure of Three-Dimensional Structure of the Alkaline Protease of Pseudomonas Aeruginosa: A Two-Domain Protein with A Calcium Binding Parallel Beta Roll Motif, PDB code: 1kap
was solved by
U.Baumann,
S.Wu,
K.M.Flaherty,
D.B.Mckay,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1kap:
The structure of Three-Dimensional Structure of the Alkaline Protease of Pseudomonas Aeruginosa: A Two-Domain Protein with A Calcium Binding Parallel Beta Roll Motif also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Three-Dimensional Structure of the Alkaline Protease of Pseudomonas Aeruginosa: A Two-Domain Protein with A Calcium Binding Parallel Beta Roll Motif
(pdb code 1kap). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Three-Dimensional Structure of the Alkaline Protease of Pseudomonas Aeruginosa: A Two-Domain Protein with A Calcium Binding Parallel Beta Roll Motif, PDB code: 1kap: Zinc binding site 1 out of 1 in 1kapGo back to![]() ![]()
Zinc binding site 1 out
of 1 in the Three-Dimensional Structure of the Alkaline Protease of Pseudomonas Aeruginosa: A Two-Domain Protein with A Calcium Binding Parallel Beta Roll Motif
![]() Mono view ![]() Stereo pair view
Reference:
U.Baumann,
S.Wu,
K.M.Flaherty,
D.B.Mckay.
Three-Dimensional Structure of the Alkaline Protease of Pseudomonas Aeruginosa: A Two-Domain Protein with A Calcium Binding Parallel Beta Roll Motif. Embo J. V. 12 3357 1993.
Page generated: Sun Oct 13 04:12:13 2024
ISSN: ISSN 0261-4189 PubMed: 8253063 |
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