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Atomistry » Calcium » PDB 7rcd-7s5k » 7ris » |
Calcium in PDB 7ris: Crystal Structure of RPA3624, A Beta-Propeller Lactonase From Rhodopseudomonas Palustris, with Active-Site Bound PhosphateEnzymatic activity of Crystal Structure of RPA3624, A Beta-Propeller Lactonase From Rhodopseudomonas Palustris, with Active-Site Bound Phosphate
All present enzymatic activity of Crystal Structure of RPA3624, A Beta-Propeller Lactonase From Rhodopseudomonas Palustris, with Active-Site Bound Phosphate:
3.1.1.17; Protein crystallography data
The structure of Crystal Structure of RPA3624, A Beta-Propeller Lactonase From Rhodopseudomonas Palustris, with Active-Site Bound Phosphate, PDB code: 7ris
was solved by
C.A.Bingman,
B.W.Hall,
R.W.Smith,
B.G.Fox,
T.J.Donohue,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 7ris:
The structure of Crystal Structure of RPA3624, A Beta-Propeller Lactonase From Rhodopseudomonas Palustris, with Active-Site Bound Phosphate also contains other interesting chemical elements:
Calcium Binding Sites:
The binding sites of Calcium atom in the Crystal Structure of RPA3624, A Beta-Propeller Lactonase From Rhodopseudomonas Palustris, with Active-Site Bound Phosphate
(pdb code 7ris). 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 Crystal Structure of RPA3624, A Beta-Propeller Lactonase From Rhodopseudomonas Palustris, with Active-Site Bound Phosphate, PDB code: 7ris: Calcium binding site 1 out of 1 in 7risGo back to![]() ![]()
Calcium binding site 1 out
of 1 in the Crystal Structure of RPA3624, A Beta-Propeller Lactonase From Rhodopseudomonas Palustris, with Active-Site Bound Phosphate
![]() Mono view ![]() Stereo pair view
Reference:
B.W.Hall,
C.A.Bingman,
B.G.Fox,
D.R.Noguera,
T.J.Donohue.
A Broad Specificity Beta-Propeller Enzyme From Rhodopseudomonas Palustris That Hydrolyzes Many Lactones Including Gamma-Valerolactone. J.Biol.Chem. 02782 2022.
Page generated: Thu Jul 10 00:48:18 2025
ISSN: ESSN 1083-351X PubMed: 36502920 DOI: 10.1016/J.JBC.2022.102782 |
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