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Calcium in PDB 2omu: Crystal Structure of Inla G194S+S Y369S/HEC1 Complex

Protein crystallography data

The structure of Crystal Structure of Inla G194S+S Y369S/HEC1 Complex, PDB code: 2omu was solved by T.Wollert, D.W.Heinz, W.D.Schubert, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.80
Space group P 1
Cell size a, b, c (Å), α, β, γ (°) 45.010, 54.273, 68.643, 74.98, 80.82, 67.36
R / Rfree (%) 16.4 / 21.7

Other elements in 2omu:

The structure of Crystal Structure of Inla G194S+S Y369S/HEC1 Complex also contains other interesting chemical elements:

Chlorine (Cl) 1 atom

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Inla G194S+S Y369S/HEC1 Complex (pdb code 2omu). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Crystal Structure of Inla G194S+S Y369S/HEC1 Complex, PDB code: 2omu:

Calcium binding site 1 out of 1 in 2omu

Go back to Calcium Binding Sites List in 2omu
Calcium binding site 1 out of 1 in the Crystal Structure of Inla G194S+S Y369S/HEC1 Complex


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Inla G194S+S Y369S/HEC1 Complex within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca1497

b:19.4
occ:0.40
OE1 A:GLU327 2.9 15.3 1.0
OD2 B:ASP29 3.1 28.0 1.0
OD1 B:ASP29 3.3 28.3 1.0
NZ B:LYS25 3.3 18.5 0.4
CG B:ASP29 3.3 27.8 1.0
O A:HOH921 3.5 35.5 1.0
OE2 A:GLU327 3.6 12.3 1.0
CD A:GLU327 3.7 13.0 1.0
CE B:LYS25 3.7 18.3 0.4
O B:HOH1529 3.8 29.7 0.6
ND2 A:ASN283 4.1 11.9 0.5
O B:HOH1572 4.2 31.9 1.0
O A:HOH806 4.4 26.8 1.0
CB B:ASP29 4.5 28.6 1.0
O B:ASP29 4.5 32.7 1.0
C B:ASP29 4.7 31.5 1.0
CB B:LYS30 4.8 36.6 1.0
CB A:ALA305 4.9 7.2 1.0
N B:LYS30 4.9 34.2 1.0

Reference:

T.Wollert, D.W.Heinz, W.D.Schubert. Thermodynamically Reengineering the Listerial Invasion Complex Inla/E-Cadherin. Proc.Natl.Acad.Sci.Usa V. 104 13960 2007.
ISSN: ISSN 0027-8424
PubMed: 17715295
DOI: 10.1073/PNAS.0702199104
Page generated: Tue Jul 8 07:21:04 2025

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