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Atomistry » Chlorine » PDB 2px2-2q6q » 2px8 » |
Chlorine in PDB 2px8: Crystal Structure of the Murray Valley Encephalitis Virus NS5 2'-O Methyltransferase Domain in Complex with Sah and 7M-GtpEnzymatic activity of Crystal Structure of the Murray Valley Encephalitis Virus NS5 2'-O Methyltransferase Domain in Complex with Sah and 7M-Gtp
All present enzymatic activity of Crystal Structure of the Murray Valley Encephalitis Virus NS5 2'-O Methyltransferase Domain in Complex with Sah and 7M-Gtp:
2.7.7.48; Protein crystallography data
The structure of Crystal Structure of the Murray Valley Encephalitis Virus NS5 2'-O Methyltransferase Domain in Complex with Sah and 7M-Gtp, PDB code: 2px8
was solved by
R.Assenberg,
J.Ren,
A.Verma,
T.S.Walter,
D.Alderton,
R.J.Hurrelbrink,
S.D.Fuller,
R.J.Owens,
D.I.Stuart,
J.M.Grimes,
Oxford Protein Productionfacility (Oppf),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of the Murray Valley Encephalitis Virus NS5 2'-O Methyltransferase Domain in Complex with Sah and 7M-Gtp
(pdb code 2px8). 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 Crystal Structure of the Murray Valley Encephalitis Virus NS5 2'-O Methyltransferase Domain in Complex with Sah and 7M-Gtp, PDB code: 2px8: Chlorine binding site 1 out of 1 in 2px8Go back to Chlorine Binding Sites List in 2px8
Chlorine binding site 1 out
of 1 in the Crystal Structure of the Murray Valley Encephalitis Virus NS5 2'-O Methyltransferase Domain in Complex with Sah and 7M-Gtp
Mono view Stereo pair view
Reference:
R.Assenberg,
J.Ren,
A.Verma,
T.S.Walter,
D.Alderton,
R.J.Hurrelbrink,
S.D.Fuller,
S.Bressanelli,
R.J.Owens,
D.I.Stuart,
J.M.Grimes.
Crystal Structure of the Murray Valley Encephalitis Virus NS5 Methyltransferase Domain in Complex with Cap Analogues. J.Gen.Virol. V. 88 2228 2007.
Page generated: Sat Dec 12 09:15:54 2020
ISSN: ISSN 0022-1317 PubMed: 17622627 DOI: 10.1099/VIR.0.82757-0 |
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