Calcium in PDB 2wii: Complement C3B in Complex with Factor H Domains 1-4

The structure of Complement C3B in Complex with Factor H Domains 1-4, PDB code: 2wii was solved by J.Wu, B.J.C.Janssen, P.Gros, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	64.48 / 2.70
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	223.489, 84.946, 128.770, 90.00, 90.00, 90.00
R / Rfree (%)	21.7 / 25.2

The binding sites of Calcium atom in the Complement C3B in Complex with Factor H Domains 1-4 (pdb code 2wii). 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 Complement C3B in Complex with Factor H Domains 1-4, PDB code: 2wii:

Calcium binding site 1 out of 1 in the Complement C3B in Complex with Factor H Domains 1-4


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Complement C3B in Complex with Factor H Domains 1-4 within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1643 b:63.8 occ:1.00 OD1 A:ASP532 2.3 44.4 1.0 O A:VAL533 2.3 38.6 1.0 OD1 A:ASP535 2.3 63.6 1.0 O A:PRO505 2.3 39.5 1.0 C A:PRO505 3.3 29.9 1.0 CG A:ASP535 3.3 64.8 1.0 CG A:ASP532 3.4 45.0 1.0 C A:VAL533 3.4 33.9 1.0 N A:VAL533 3.6 30.3 1.0 CB A:PRO505 3.7 33.4 1.0 CA A:PRO505 3.8 30.8 1.0 OD2 A:ASP535 3.8 71.6 1.0 OD2 A:ASP532 3.9 60.5 1.0 O A:HOH2055 4.0 34.0 1.0 CA A:VAL533 4.0 37.9 1.0 N A:ASP535 4.3 51.8 1.0 N A:SER506 4.4 33.3 1.0 N A:LYS534 4.5 38.2 1.0 CB A:ASP535 4.5 58.2 1.0 C A:ASP532 4.5 33.9 1.0 CB A:SER506 4.5 30.0 1.0 C A:LYS534 4.6 46.0 1.0 CB A:ASP532 4.6 33.2 1.0 CA A:ASP535 4.7 54.6 1.0 O A:HOH2054 4.7 42.9 1.0 CB A:VAL533 4.7 30.9 1.0 CA A:ASP532 4.7 36.4 1.0 CA A:SER506 4.8 31.7 1.0 CA A:LYS534 4.8 47.7 1.0

J.Wu, Y.Q.Wu, D.Ricklin, B.J.Janssen, J.D.Lambris, P.Gros. Structure of Complement Fragment C3B-Factor H and Implications For Host Protection By Complement Regulators. Nat. Immunol. V. 10 728 2009.
ISSN: ESSN 1529-2916
PubMed: 19503104
DOI: 10.1038/NI.1755