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Atomistry » Cobalt » PDB 2o5s-2r2s » 2r1n | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Cobalt » PDB 2o5s-2r2s » 2r1n » |
Cobalt in PDB 2r1n: Opda From Agrobacterium Radiobacter with Bound Slow Substrate Diethyl 4-Methoxyphenyl Phosphate (20H)- 1.7 AEnzymatic activity of Opda From Agrobacterium Radiobacter with Bound Slow Substrate Diethyl 4-Methoxyphenyl Phosphate (20H)- 1.7 A
All present enzymatic activity of Opda From Agrobacterium Radiobacter with Bound Slow Substrate Diethyl 4-Methoxyphenyl Phosphate (20H)- 1.7 A:
3.1.8.1; Protein crystallography data
The structure of Opda From Agrobacterium Radiobacter with Bound Slow Substrate Diethyl 4-Methoxyphenyl Phosphate (20H)- 1.7 A, PDB code: 2r1n
was solved by
D.L.Ollis,
C.J.Jackson,
J.L.Foo,
H.K.Kim,
P.D.Carr,
J.W.Liu,
G.Salem,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2r1n:
The structure of Opda From Agrobacterium Radiobacter with Bound Slow Substrate Diethyl 4-Methoxyphenyl Phosphate (20H)- 1.7 A also contains other interesting chemical elements:
Cobalt Binding Sites:
The binding sites of Cobalt atom in the Opda From Agrobacterium Radiobacter with Bound Slow Substrate Diethyl 4-Methoxyphenyl Phosphate (20H)- 1.7 A
(pdb code 2r1n). This binding sites where shown within
5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Opda From Agrobacterium Radiobacter with Bound Slow Substrate Diethyl 4-Methoxyphenyl Phosphate (20H)- 1.7 A, PDB code: 2r1n: Cobalt binding site 1 out of 1 in 2r1nGo back to![]() ![]()
Cobalt binding site 1 out
of 1 in the Opda From Agrobacterium Radiobacter with Bound Slow Substrate Diethyl 4-Methoxyphenyl Phosphate (20H)- 1.7 A
![]() Mono view ![]() Stereo pair view
Reference:
C.J.Jackson,
J.L.Foo,
H.K.Kim,
P.D.Carr,
J.W.Liu,
G.Salem,
D.L.Ollis.
In Crystallo Capture of A Michaelis Complex and Product-Binding Modes of A Bacterial Phosphotriesterase J.Mol.Biol. V. 375 1189 2008.
Page generated: Sun Jul 13 18:29:15 2025
ISSN: ISSN 0022-2836 PubMed: 18082180 DOI: 10.1016/J.JMB.2007.10.061 |
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