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Calcium in PDB 4a5w: Crystal Structure of C5B6

Protein crystallography data

The structure of Crystal Structure of C5B6, PDB code: 4a5w was solved by M.A.Hadders, D.Bubeck, F.Forneris, M.Pangburn, O.Llorca, S.M.Lea, P.Gros, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.19 / 3.50
Space group I 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 154.217, 230.747, 269.983, 90.00, 90.00, 90.00
R / Rfree (%) 25.6 / 27

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of C5B6 (pdb code 4a5w). 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 Crystal Structure of C5B6, PDB code: 4a5w:

Calcium binding site 1 out of 1 in 4a5w

Go back to Calcium Binding Sites List in 4a5w
Calcium binding site 1 out of 1 in the Crystal Structure of C5B6


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 C5B6 within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca1000

b:0.6
occ:1.00
OD1 B:ASP172 2.8 0.0 1.0
O B:ASN159 3.2 0.9 1.0
N B:ASN162 3.4 0.2 1.0
O B:LEU156 3.4 0.7 1.0
CB B:LEU156 3.4 0.6 1.0
CA B:ASN162 3.5 0.5 1.0
C B:LEU156 3.8 0.4 1.0
C B:ASN159 3.8 0.9 1.0
CG B:ASP172 3.9 0.6 1.0
CD2 B:LEU156 3.9 0.9 1.0
CG B:LEU156 4.0 0.1 1.0
O B:CYS158 4.0 0.6 1.0
CA B:LEU156 4.1 0.9 1.0
N B:GLY160 4.3 0.3 1.0
N B:ASP163 4.4 0.3 1.0
C B:ASN162 4.4 0.1 1.0
C B:CYS158 4.4 0.6 1.0
CB B:ASN162 4.5 0.8 1.0
N B:GLU157 4.5 0.3 1.0
OD2 B:ASP172 4.5 0.9 1.0
C B:GLU161 4.6 0.5 1.0
N B:ASN159 4.6 0.9 1.0
CA B:ASN159 4.6 0.5 1.0
N B:GLU161 4.7 0.9 1.0
CB B:ASP172 4.9 0.3 1.0
CA B:GLU157 5.0 0.3 1.0

Reference:

M.A.Hadders, D.Bubeck, P.Roversi, S.Hakobyan, F.Forneris, B.P.Morgan, M.K.Pangburn, O.Llorca, S.M.Lea, P.Gros. Assembly and Regulation of the Membrane Attack Complex Based on Structures of C5B6 and SC5B9. Cell Rep. V. 1 200 2012.
ISSN: ESSN 2211-1247
PubMed: 22832194
DOI: 10.1016/J.CELREP.2012.02.003
Page generated: Sat Dec 12 04:38:10 2020

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