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Chlorine in PDB 6g5v: The X-Ray Structure of the Adduct Formed in the Reaction Between Lysozyme and A Platinum(II) Terpyridine Compound (pH 7.0)Enzymatic activity of The X-Ray Structure of the Adduct Formed in the Reaction Between Lysozyme and A Platinum(II) Terpyridine Compound (pH 7.0)
All present enzymatic activity of The X-Ray Structure of the Adduct Formed in the Reaction Between Lysozyme and A Platinum(II) Terpyridine Compound (pH 7.0):
3.2.1.17; Protein crystallography data
The structure of The X-Ray Structure of the Adduct Formed in the Reaction Between Lysozyme and A Platinum(II) Terpyridine Compound (pH 7.0), PDB code: 6g5v
was solved by
A.Merlino,
G.Ferraro,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6g5v:
The structure of The X-Ray Structure of the Adduct Formed in the Reaction Between Lysozyme and A Platinum(II) Terpyridine Compound (pH 7.0) also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the The X-Ray Structure of the Adduct Formed in the Reaction Between Lysozyme and A Platinum(II) Terpyridine Compound (pH 7.0)
(pdb code 6g5v). 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 The X-Ray Structure of the Adduct Formed in the Reaction Between Lysozyme and A Platinum(II) Terpyridine Compound (pH 7.0), PDB code: 6g5v: Chlorine binding site 1 out of 1 in 6g5vGo back to Chlorine Binding Sites List in 6g5v
Chlorine binding site 1 out
of 1 in the The X-Ray Structure of the Adduct Formed in the Reaction Between Lysozyme and A Platinum(II) Terpyridine Compound (pH 7.0)
Mono view Stereo pair view
Reference:
G.Ferraro,
T.Marzo,
T.Infrasca,
A.Cilibrizzi,
R.Vilar,
L.Messori,
A.Merlino.
A Case of Extensive Protein Platination: the Reaction of Lysozyme with A Pt(II)-Terpyridine Complex. Dalton Trans V. 47 8716 2018.
Page generated: Sat Dec 12 13:00:45 2020
ISSN: ESSN 1477-9234 PubMed: 29904761 DOI: 10.1039/C8DT01254G |
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