Calcium in PDB 2ice: Crig Bound to C3C

The structure of Crig Bound to C3C, PDB code: 2ice was solved by C.Wiesmann, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 3.10
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	384.936, 65.213, 147.676, 90.00, 102.91, 90.00
R / Rfree (%)	23.6 / 29.5

The binding sites of Calcium atom in the Crig Bound to C3C (pdb code 2ice). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crig Bound to C3C, PDB code: 2ice:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crig Bound to C3C


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crig Bound to C3C within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca645 b:37.5 occ:1.00 OD1 A:ASP535 2.2 47.6 1.0 O A:PRO505 2.4 29.7 1.0 O A:VAL533 2.4 35.7 1.0 OD1 A:ASP532 2.5 30.7 1.0 CG A:ASP535 3.2 48.2 1.0 C A:PRO505 3.4 29.9 1.0 C A:VAL533 3.6 30.3 1.0 CG A:ASP532 3.6 31.2 1.0 OD2 A:ASP535 3.9 53.7 1.0 N A:ASP535 3.9 41.9 1.0 CA A:PRO505 3.9 29.0 1.0 CB A:PRO505 4.0 27.1 1.0 OD2 A:ASP532 4.1 33.7 1.0 CB A:ASP535 4.3 44.6 1.0 C A:LYS534 4.3 39.6 1.0 OE1 A:GLU599 4.4 60.2 1.0 CA A:ASP535 4.4 40.8 1.0 N A:VAL533 4.5 23.4 1.0 N A:LYS534 4.5 34.6 1.0 CA A:LYS534 4.5 37.5 1.0 CA A:VAL533 4.6 23.1 1.0 N A:SER506 4.6 25.4 1.0 C A:ASP532 4.6 29.3 1.0 CB A:SER506 4.7 26.6 1.0 CB A:ASP532 4.9 29.3 1.0 CA A:ASP532 5.0 29.8 1.0 O A:LYS534 5.0 42.7 1.0

Calcium binding site 2 out of 2 in the Crig Bound to C3C


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crig Bound to C3C within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca643 b:64.1 occ:1.00 O D:PRO505 2.0 29.8 1.0 OD1 D:ASP535 2.3 47.8 1.0 OD1 D:ASP532 2.4 30.8 1.0 O D:VAL533 2.5 35.4 1.0 C D:PRO505 3.1 29.7 1.0 CG D:ASP535 3.4 48.4 1.0 CG D:ASP532 3.6 31.2 1.0 CB D:PRO505 3.7 27.0 1.0 CA D:PRO505 3.7 28.7 1.0 C D:VAL533 3.7 30.4 1.0 OE1 D:GLU599 4.0 60.2 1.0 OD2 D:ASP535 4.0 53.6 1.0 OD2 D:ASP532 4.2 33.7 1.0 N D:SER506 4.2 25.8 1.0 CB D:SER506 4.3 26.7 1.0 N D:ASP535 4.3 41.7 1.0 N D:VAL533 4.4 23.8 1.0 CB D:ASP535 4.6 44.8 1.0 CA D:VAL533 4.6 23.4 1.0 C D:LYS534 4.6 39.6 1.0 C D:ASP532 4.6 29.2 1.0 CA D:SER506 4.7 26.4 1.0 N D:LYS534 4.7 34.8 1.0 CA D:ASP535 4.7 40.9 1.0 CB D:ASP532 4.8 29.4 1.0 CA D:LYS534 4.8 37.8 1.0 CA D:ASP532 4.8 29.7 1.0 CG D:PRO505 4.9 25.3 1.0 CB D:VAL533 5.0 20.5 1.0

C.Wiesmann, K.J.Katschke, J.Yin, K.Y.Helmy, M.Steffek, W.J.Fairbrother, S.A.Mccallum, L.Embuscado, L.Deforge, P.E.Hass, M.Van Lookeren Campagne. Structure of C3B in Complex with Crig Gives Insights Into Regulation of Complement Activation. Nature V. 444 217 2006.
ISSN: ISSN 0028-0836
PubMed: 17051150
DOI: 10.1038/NATURE05263