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Calcium in PDB 2j5w: Ceruloplasmin Revisited: Structural and Functional Roles of Various Metal Cation Binding Sites

Enzymatic activity of Ceruloplasmin Revisited: Structural and Functional Roles of Various Metal Cation Binding Sites

All present enzymatic activity of Ceruloplasmin Revisited: Structural and Functional Roles of Various Metal Cation Binding Sites:
1.16.3.1;

Protein crystallography data

The structure of Ceruloplasmin Revisited: Structural and Functional Roles of Various Metal Cation Binding Sites, PDB code: 2j5w was solved by I.Bento, C.Peixoto, V.N.Zaitsev, P.F.Lindley, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 68.52 / 2.80
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 209.140, 209.139, 82.752, 90.00, 90.00, 120.00
R / Rfree (%) 17.5 / 22.6

Other elements in 2j5w:

The structure of Ceruloplasmin Revisited: Structural and Functional Roles of Various Metal Cation Binding Sites also contains other interesting chemical elements:

Copper (Cu) 7 atoms
Sodium (Na) 3 atoms

Calcium Binding Sites:

The binding sites of Calcium atom in the Ceruloplasmin Revisited: Structural and Functional Roles of Various Metal Cation Binding Sites (pdb code 2j5w). 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 Ceruloplasmin Revisited: Structural and Functional Roles of Various Metal Cation Binding Sites, PDB code: 2j5w:

Calcium binding site 1 out of 1 in 2j5w

Go back to Calcium Binding Sites List in 2j5w
Calcium binding site 1 out of 1 in the Ceruloplasmin Revisited: Structural and Functional Roles of Various Metal Cation Binding Sites


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Ceruloplasmin Revisited: Structural and Functional Roles of Various Metal Cation Binding Sites within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca3042

b:43.8
occ:1.00
 OD2 A:ASP128 2.2 41.7 1.0
O A:HOH2025 2.3 44.0 1.0
O A:LYS109 2.4 43.2 1.0
O A:GLN124 2.4 42.2 1.0
OD1 A:ASP127 2.5 45.5 1.0
OD2 A:ASP127 2.5 44.3 1.0
OD1 A:ASP128 2.5 44.4 1.0
O A:HOH2030 2.5 33.8 1.0
CG A:ASP128 2.7 43.8 1.0
CG A:ASP127 2.8 44.8 1.0
C A:LYS109 3.5 43.7 1.0
C A:GLN124 3.6 42.9 1.0
CB A:ASP128 4.2 43.9 1.0
CA A:ARG125 4.3 42.9 1.0
O A:ALA114 4.3 39.0 1.0
N A:ARG125 4.3 42.9 1.0
CB A:ASP127 4.3 44.5 1.0
O A:HOH2026 4.4 39.2 1.0
N A:GLU110 4.4 43.5 1.0
CA A:LYS109 4.5 43.9 1.0
CA A:GLU110 4.5 43.3 1.0
CB A:GLU112 4.6 40.5 1.0
N A:ASP128 4.6 44.1 1.0
C A:GLU110 4.7 43.0 1.0
CA A:GLN124 4.7 43.3 1.0
N A:GLY113 4.7 39.8 1.0
N A:GLU112 4.7 40.9 1.0
CB A:LYS109 4.7 43.7 1.0
OD2 A:ASP118 4.8 38.4 1.0
C A:ARG125 4.9 43.0 1.0
OE1 A:GLU112 4.9 40.5 1.0
CB A:GLN124 4.9 43.2 1.0
CA A:ASP128 5.0 44.1 1.0
N A:HIS111 5.0 42.8 1.0

Reference:

I.Bento, C.Peixoto, V.N.Zaitsev, P.F.Lindley. Ceruloplasmin Revisited: Structural and Functional Roles of Various Metal Cation-Binding Sites. Acta Crystallogr.,Sect.D V. 63 240 2007.
ISSN: ISSN 0907-4449
PubMed: 17242517
DOI: 10.1107/S090744490604947X
Page generated: Fri Jul 12 13:27:32 2024

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