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Calcium in PDB 2fps: Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Apo Ca Model.

Enzymatic activity of Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Apo Ca Model.

All present enzymatic activity of Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Apo Ca Model.:
3.1.3.15;

Protein crystallography data

The structure of Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Apo Ca Model., PDB code: 2fps was solved by E.S.Rangarajan, M.Cygler, A.Matte, Montreal-Kingston Bacterialstructural Genomics Initiative (Bsgi), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.20
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 52.748, 131.325, 104.898, 90.00, 90.00, 90.00
R / Rfree (%) 17 / 24.4

Other elements in 2fps:

The structure of Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Apo Ca Model. also contains other interesting chemical elements:

Chlorine (Cl) 2 atoms
Zinc (Zn) 2 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Apo Ca Model. (pdb code 2fps). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Apo Ca Model., PDB code: 2fps:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 2fps

Go back to Calcium Binding Sites List in 2fps
Calcium binding site 1 out of 2 in the Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Apo Ca Model.


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 the N-Terminal Domain of E.Coli Hisb- Apo Ca Model. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca503

b:17.7
occ:1.00
O A:ASP12 2.3 12.1 1.0
OD1 A:ASP131 2.3 15.2 1.0
O A:HOH529 2.3 16.1 1.0
O A:HOH509 2.3 13.3 1.0
OD2 A:ASP10 2.4 12.4 1.0
O A:HOH528 2.4 10.6 1.0
CG A:ASP10 3.2 14.2 1.0
CG A:ASP131 3.3 15.4 1.0
OD1 A:ASP10 3.3 14.7 1.0
C A:ASP12 3.5 12.4 1.0
OD2 A:ASP131 3.6 15.1 1.0
O A:HOH508 4.1 13.9 1.0
CD A:ARG132 4.2 18.8 1.0
NE A:ARG132 4.3 22.2 1.0
OG1 A:THR14 4.3 11.7 1.0
CG A:ARG132 4.3 16.6 1.0
OD2 A:ASP135 4.4 14.7 1.0
N A:GLY13 4.4 11.9 1.0
CA A:GLY13 4.4 12.1 1.0
CA A:ASP12 4.4 13.3 1.0
OE2 A:GLU18 4.5 21.0 1.0
CL A:CL505 4.5 27.1 1.0
O A:HOH559 4.5 26.3 1.0
CB A:ASP10 4.5 13.6 1.0
N A:ASP12 4.5 13.4 1.0
CB A:ASP12 4.6 13.7 1.0
CB A:ASP131 4.6 15.3 1.0
N A:ASP131 4.7 14.9 1.0
C A:GLY13 4.8 12.0 1.0
N A:ARG132 5.0 15.8 1.0
CB A:ARG132 5.0 16.9 1.0

Calcium binding site 2 out of 2 in 2fps

Go back to Calcium Binding Sites List in 2fps
Calcium binding site 2 out of 2 in the Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Apo Ca Model.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of the N-Terminal Domain of E.Coli Hisb- Apo Ca Model. within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca504

b:18.7
occ:1.00
OD1 B:ASP131 2.3 15.7 1.0
O B:ASP12 2.3 13.7 1.0
OD2 B:ASP10 2.3 17.6 1.0
O B:HOH515 2.3 13.3 1.0
O B:HOH527 2.3 19.8 1.0
O B:HOH539 2.5 14.1 1.0
CG B:ASP10 3.2 14.4 1.0
CG B:ASP131 3.3 15.3 1.0
OD1 B:ASP10 3.4 15.4 1.0
C B:ASP12 3.5 14.0 1.0
OD2 B:ASP131 3.6 16.9 1.0
O B:HOH528 4.2 15.1 1.0
CG B:ARG132 4.2 19.5 1.0
OD2 B:ASP135 4.3 16.8 1.0
OG1 B:THR14 4.3 12.4 1.0
NE B:ARG132 4.4 29.2 1.0
N B:GLY13 4.4 13.0 1.0
CA B:ASP12 4.4 14.7 1.0
O B:HOH678 4.4 17.6 1.0
CA B:GLY13 4.4 12.8 1.0
N B:ASP12 4.5 14.3 1.0
CL B:CL506 4.5 28.5 1.0
CB B:ASP10 4.5 14.0 1.0
CB B:ASP12 4.6 14.6 1.0
CD B:ARG132 4.6 26.3 1.0
CB B:ASP131 4.7 15.0 1.0
N B:ASP131 4.7 14.9 1.0
OE2 B:GLU18 4.7 15.1 1.0
C B:GLY13 4.8 12.4 1.0
O B:HOH541 4.9 17.1 1.0
N B:THR14 5.0 12.0 1.0

Reference:

E.S.Rangarajan, A.Proteau, J.Wagner, M.N.Hung, A.Matte, M.Cygler. Structural Snapshots of Escherichia Coli Histidinol Phosphate Phosphatase Along the Reaction Pathway. J.Biol.Chem. V. 281 37930 2006.
ISSN: ISSN 0021-9258
PubMed: 16966333
DOI: 10.1074/JBC.M604916200
Page generated: Sat Dec 12 03:37:35 2020

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