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Atomistry » Chlorine » PDB 7sqe-7t2x » 7t1l | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 7sqe-7t2x » 7t1l » |
Chlorine in PDB 7t1l: Crystal Structure of A Superbinder Fes SH2 Domain (Sfess) in Complex with A High Affinity PhosphopeptideEnzymatic activity of Crystal Structure of A Superbinder Fes SH2 Domain (Sfess) in Complex with A High Affinity Phosphopeptide
All present enzymatic activity of Crystal Structure of A Superbinder Fes SH2 Domain (Sfess) in Complex with A High Affinity Phosphopeptide:
2.7.10.2; Protein crystallography data
The structure of Crystal Structure of A Superbinder Fes SH2 Domain (Sfess) in Complex with A High Affinity Phosphopeptide, PDB code: 7t1l
was solved by
G.D.Martyn,
A.U.Singer,
G.Veggiani,
I.Kurinov,
F.Sicheri,
S.S.Sidhu,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 7t1l:
The structure of Crystal Structure of A Superbinder Fes SH2 Domain (Sfess) in Complex with A High Affinity Phosphopeptide also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of A Superbinder Fes SH2 Domain (Sfess) in Complex with A High Affinity Phosphopeptide
(pdb code 7t1l). 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 A Superbinder Fes SH2 Domain (Sfess) in Complex with A High Affinity Phosphopeptide, PDB code: 7t1l: Chlorine binding site 1 out of 1 in 7t1lGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Crystal Structure of A Superbinder Fes SH2 Domain (Sfess) in Complex with A High Affinity Phosphopeptide
![]() Mono view ![]() Stereo pair view
Reference:
G.D.Martyn,
G.Veggiani,
U.Kusebauch,
S.R.Morrone,
B.P.Yates,
A.U.Singer,
J.Tong,
N.Manczyk,
G.Gish,
Z.Sun,
I.Kurinov,
F.Sicheri,
M.F.Moran,
R.L.Moritz,
S.S.Sidhu.
Engineered SH2 Domains For Targeted Phosphoproteomics. Acs Chem.Biol. V. 17 1472 2022.
Page generated: Sun Jul 13 07:17:18 2025
ISSN: ESSN 1554-8937 PubMed: 35613471 DOI: 10.1021/ACSCHEMBIO.2C00051 |
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