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Atomistry » Magnesium » PDB 3cfx-3cpj » 3cly » |
Magnesium in PDB 3cly: Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domains Trapped in Trans-Phosphorylation ReactionEnzymatic activity of Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domains Trapped in Trans-Phosphorylation Reaction
All present enzymatic activity of Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domains Trapped in Trans-Phosphorylation Reaction:
2.7.10.1; Protein crystallography data
The structure of Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domains Trapped in Trans-Phosphorylation Reaction, PDB code: 3cly
was solved by
H.Chen,
M.Mohammadi,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domains Trapped in Trans-Phosphorylation Reaction
(pdb code 3cly). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domains Trapped in Trans-Phosphorylation Reaction, PDB code: 3cly: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 3clyGo back to Magnesium Binding Sites List in 3cly
Magnesium binding site 1 out
of 2 in the Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domains Trapped in Trans-Phosphorylation Reaction
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 3clyGo back to Magnesium Binding Sites List in 3cly
Magnesium binding site 2 out
of 2 in the Crystal Structure of Fgf Receptor 2 (FGFR2) Kinase Domains Trapped in Trans-Phosphorylation Reaction
Mono view Stereo pair view
Reference:
H.Chen,
C.F.Xu,
J.Ma,
A.V.Eliseenkova,
W.Li,
P.M.Pollock,
N.Pitteloud,
W.T.Miller,
T.A.Neubert,
M.Mohammadi.
A Crystallographic Snapshot of Tyrosine Trans-Phosphorylation in Action Proc.Natl.Acad.Sci.Usa V. 105 19660 2008.
Page generated: Wed Aug 14 11:25:53 2024
ISSN: ISSN 0027-8424 PubMed: 19060208 DOI: 10.1073/PNAS.0807752105 |
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