Calcium in PDB 2w86: Crystal Structure of Fibrillin-1 Domains CBEGF9HYB2CBEGF10, Calcium Saturated Form

The structure of Crystal Structure of Fibrillin-1 Domains CBEGF9HYB2CBEGF10, Calcium Saturated Form, PDB code: 2w86 was solved by S.A.Jensen, S.Iqbal, E.D.Lowe, C.Redfield, P.A.Handford, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.750 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	31.232, 47.258, 89.105, 90.00, 90.00, 90.00
R / Rfree (%)	18.51 / 22.12

The structure of Crystal Structure of Fibrillin-1 Domains CBEGF9HYB2CBEGF10, Calcium Saturated Form also contains other interesting chemical elements:

Iodine

(I)

3 atoms

The binding sites of Calcium atom in the Crystal Structure of Fibrillin-1 Domains CBEGF9HYB2CBEGF10, Calcium Saturated Form (pdb code 2w86). 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 Fibrillin-1 Domains CBEGF9HYB2CBEGF10, Calcium Saturated Form, PDB code: 2w86:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Fibrillin-1 Domains CBEGF9HYB2CBEGF10, Calcium Saturated Form


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 Fibrillin-1 Domains CBEGF9HYB2CBEGF10, Calcium Saturated Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1148 b:19.7 occ:1.00 O A:ILE4 2.4 16.7 1.0 OD1 A:ASN19 2.4 17.5 1.0 OE2 A:GLU6 2.5 19.3 1.0 O A:SER23 2.6 17.4 1.0 O A:SER20 2.6 19.2 1.0 OD1 A:ASP3 2.6 20.0 1.0 OD2 A:ASP3 2.9 21.4 1.0 CG A:ASP3 3.1 19.1 1.0 CG A:ASN19 3.4 22.6 1.0 CD A:GLU6 3.5 21.7 1.0 C A:SER23 3.6 25.8 1.0 C A:ILE4 3.6 15.6 1.0 N A:SER23 3.6 24.9 1.0 OE1 A:GLU6 3.7 22.4 1.0 C A:SER20 3.8 24.0 1.0 ND2 A:ASN19 3.8 21.2 1.0 N A:SER20 4.0 21.2 1.0 CA A:SER23 4.0 25.7 1.0 N A:GLY22 4.1 32.7 1.0 N A:ILE4 4.3 15.6 1.0 C A:GLY22 4.3 27.9 1.0 CA A:ILE4 4.4 14.3 1.0 N A:GLU6 4.5 18.6 1.0 CB A:ASP3 4.5 14.8 1.0 CA A:SER20 4.5 24.9 1.0 N A:ASP5 4.5 16.1 1.0 CA A:GLY22 4.6 31.1 1.0 CA A:ASP5 4.6 19.7 1.0 N A:PHE24 4.7 20.6 1.0 CB A:ASN19 4.7 19.8 1.0 CB A:ILE4 4.7 12.9 1.0 N A:PRO21 4.8 28.5 1.0 C A:PRO21 4.8 30.6 1.0 C A:ASP3 4.8 15.6 1.0 CA A:PRO21 4.8 30.9 1.0 CG A:GLU6 4.9 17.9 1.0 C A:ASN19 4.9 22.0 1.0 CA A:ASN19 4.9 17.9 1.0 O A:HOH2007 5.0 37.7 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Fibrillin-1 Domains CBEGF9HYB2CBEGF10, Calcium Saturated Form


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 Fibrillin-1 Domains CBEGF9HYB2CBEGF10, Calcium Saturated Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1149 b:14.9 occ:1.00 OD1 A:ASN124 2.4 12.8 1.0 O A:ILE107 2.4 13.5 1.0 O A:SER128 2.4 14.8 1.0 OD1 A:ASP106 2.5 14.3 1.0 O A:HOH2110 2.5 13.5 1.0 OE1 A:GLU109 2.5 12.3 1.0 O A:THR125 2.5 15.2 1.0 CG A:ASP106 3.2 18.0 1.0 OD2 A:ASP106 3.2 16.2 1.0 CG A:ASN124 3.4 14.8 1.0 CD A:GLU109 3.4 15.4 1.0 C A:SER128 3.5 15.9 1.0 C A:ILE107 3.6 15.8 1.0 N A:SER128 3.7 11.4 1.0 OE2 A:GLU109 3.7 18.2 1.0 C A:THR125 3.7 13.9 1.0 ND2 A:ASN124 3.8 14.0 1.0 N A:GLY127 3.9 13.5 1.0 N A:THR125 4.0 14.7 1.0 CA A:SER128 4.0 16.1 1.0 C A:GLY127 4.3 14.3 1.0 N A:GLU109 4.3 15.0 1.0 N A:ILE107 4.3 13.7 1.0 CA A:ASP108 4.3 15.5 1.0 N A:ASP108 4.4 13.8 1.0 CA A:GLY127 4.5 13.5 1.0 CA A:ILE107 4.6 15.3 1.0 CA A:THR125 4.6 13.5 1.0 O A:GLY95 4.6 12.1 1.0 N A:PHE129 4.6 12.7 1.0 C A:ARG126 4.6 15.8 1.0 CA A:ARG126 4.7 12.2 1.0 CB A:ASP106 4.7 16.4 1.0 N A:ARG126 4.7 13.8 1.0 CB A:ASN124 4.7 13.6 1.0 CG A:GLU109 4.8 16.0 1.0 C A:ASP108 4.9 14.4 1.0 C A:ASN124 4.9 15.9 1.0 CA A:ASN124 4.9 16.2 1.0 OG1 A:THR125 4.9 18.1 1.0 CB A:PHE129 4.9 12.6 1.0

S.A.Jensen, S.Iqbal, E.D.Lowe, C.Redfield, P.A.Handford. Structure and Interdomain Interactions of A Hybrid Domain: A Disulphide-Rich Module of the Fibrillin/Ltbp Superfamily of Matrix Proteins. Structure V. 17 759 2009.
ISSN: ISSN 0969-2126
PubMed: 19446531
DOI: 10.1016/J.STR.2009.03.014