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Calcium in PDB 2fha: Human H Chain Ferritin

Protein crystallography data

The structure of Human H Chain Ferritin, PDB code: 2fha was solved by P.D.Hempstead, P.J.Artymiuk, P.M.Harrison, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.90
Space group F 4 3 2
Cell size a, b, c (Å), α, β, γ (°) 184.800, 184.800, 184.800, 90.00, 90.00, 90.00
R / Rfree (%) 18.6 / n/a

Calcium Binding Sites:

The binding sites of Calcium atom in the Human H Chain Ferritin (pdb code 2fha). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Human H Chain Ferritin, PDB code: 2fha:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 2fha

Go back to Calcium Binding Sites List in 2fha
Calcium binding site 1 out of 2 in the Human H Chain Ferritin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Human H Chain Ferritin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca210

b:34.0
occ:0.50
OE1 A:GLN86 3.1 35.5 1.0
CD A:GLN86 4.2 24.3 1.0
O A:HOH2546 4.3 37.4 1.0
NE2 A:GLN86 4.7 33.3 1.0

Calcium binding site 2 out of 2 in 2fha

Go back to Calcium Binding Sites List in 2fha
Calcium binding site 2 out of 2 in the Human H Chain Ferritin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Human H Chain Ferritin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca211

b:69.0
occ:0.33
OD1 A:ASP131 2.6 42.8 1.0
OE1 A:GLU134 2.8 57.6 1.0
CG A:ASP131 3.8 0.0 1.0
CD A:GLU134 4.1 28.9 1.0
CB A:ASP131 4.6 28.5 1.0
OD2 A:ASP131 4.7 32.8 1.0
OE2 A:GLU134 4.8 41.7 1.0
CB A:GLU134 4.9 22.3 1.0
CA A:ASP131 4.9 23.3 1.0

Reference:

P.D.Hempstead, S.J.Yewdall, A.R.Fernie, D.M.Lawson, P.J.Artymiuk, D.W.Rice, G.C.Ford, P.M.Harrison. Comparison of the Three-Dimensional Structures of Recombinant Human H and Horse L Ferritins at High Resolution. J.Mol.Biol. V. 268 424 1997.
ISSN: ISSN 0022-2836
PubMed: 9159481
DOI: 10.1006/JMBI.1997.0970
Page generated: Fri Jul 12 10:27:44 2024

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