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Atomistry » Chlorine » PDB 4rsh-4s27 » 4rw2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 4rsh-4s27 » 4rw2 » |
Chlorine in PDB 4rw2: Hen Egg-White Lysozyme Structure From A Spent-Beam Experiment at Lcls: Refocused BeamEnzymatic activity of Hen Egg-White Lysozyme Structure From A Spent-Beam Experiment at Lcls: Refocused Beam
All present enzymatic activity of Hen Egg-White Lysozyme Structure From A Spent-Beam Experiment at Lcls: Refocused Beam:
3.2.1.17; Protein crystallography data
The structure of Hen Egg-White Lysozyme Structure From A Spent-Beam Experiment at Lcls: Refocused Beam, PDB code: 4rw2
was solved by
S.Boutet,
L.Foucar,
T.Barends,
R.B.Doak,
J.E.Koglin,
M.Messerschmidt,
K.Nass,
I.Schlichting,
R.Shoeman,
G.J.Williams,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4rw2:
The structure of Hen Egg-White Lysozyme Structure From A Spent-Beam Experiment at Lcls: Refocused Beam also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Hen Egg-White Lysozyme Structure From A Spent-Beam Experiment at Lcls: Refocused Beam
(pdb code 4rw2). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Hen Egg-White Lysozyme Structure From A Spent-Beam Experiment at Lcls: Refocused Beam, PDB code: 4rw2: Chlorine binding site 1 out of 1 in 4rw2Go back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Hen Egg-White Lysozyme Structure From A Spent-Beam Experiment at Lcls: Refocused Beam
![]() Mono view ![]() Stereo pair view
Reference:
S.Boutet,
L.Foucar,
T.R.Barends,
S.Botha,
R.B.Doak,
J.E.Koglin,
M.Messerschmidt,
K.Nass,
I.Schlichting,
M.M.Seibert,
R.L.Shoeman,
G.J.Williams.
Characterization and Use of the Spent Beam For Serial Operation of Lcls. J.Synchrotron Radiat. V. 22 634 2015.
Page generated: Fri Jul 26 01:36:13 2024
ISSN: ISSN 0909-0495 PubMed: 25931079 DOI: 10.1107/S1600577515004002 |
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