Calcium in PDB 5ebc: Crystal Structure of ECCB1 of Mycobacterium Tuberculosis in Spacegroup P21 (State III)

Protein crystallography data

The structure of Crystal Structure of ECCB1 of Mycobacterium Tuberculosis in Spacegroup P21 (State III), PDB code: 5ebc was solved by X.L.Zhang, C.Qi, X.Q.Xie, D.F.Li, L.J.Bi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 30.28 / 3.00
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 31.610, 120.210, 61.260, 90.00, 102.92, 90.00
R / Rfree (%) 23.2 / 28.6

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of ECCB1 of Mycobacterium Tuberculosis in Spacegroup P21 (State III) (pdb code 5ebc). 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 ECCB1 of Mycobacterium Tuberculosis in Spacegroup P21 (State III), PDB code: 5ebc:

Calcium binding site 1 out of 1 in 5ebc

Go back to Calcium Binding Sites List in 5ebc
Calcium binding site 1 out of 1 in the Crystal Structure of ECCB1 of Mycobacterium Tuberculosis in Spacegroup P21 (State III)


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 ECCB1 of Mycobacterium Tuberculosis in Spacegroup P21 (State III) within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca501

b:0.1
occ:1.00
OE1 A:GLU114 3.1 63.0 1.0
OD1 A:ASP108 3.2 59.5 1.0
OD2 A:ASP108 3.2 50.8 1.0
OE2 A:GLU114 3.5 61.2 1.0
NE2 A:GLN111 3.5 0.1 1.0
CG A:ASP108 3.6 54.6 1.0
CD A:GLU114 3.7 61.8 1.0
CD A:GLN111 4.6 0.2 1.0
O A:ASP108 4.6 57.2 1.0
O A:SER292 4.7 55.0 1.0
CG A:GLN111 4.8 93.9 1.0
OD2 A:ASP270 4.8 65.7 1.0
O A:PRO109 4.8 55.2 1.0

Reference:

X.Q.Xie, X.L.Zhang, C.Qi, D.F.Li, J.Fleming, D.C.Wang, L.J.Bi. Crystallographic Observation of the Movement of the Membrane-Distal Domain of the T7SS Core Component ECCB1 From Mycobacterium Tuberculosis. Acta Crystallogr.,Sect.F V. 72 139 2016.
ISSN: ESSN 2053-230X
PubMed: 26841765
DOI: 10.1107/S2053230X16000212
Page generated: Sat Dec 12 05:23:13 2020

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