Calcium in PDB 3ch2: Crystal Structure Analysis of SERA5E From Plasmodium Falciparum

The structure of Crystal Structure Analysis of SERA5E From Plasmodium Falciparum, PDB code: 3ch2 was solved by B.J.Smith, R.L.Malby, P.M.Colman, O.B.Clarke, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.46 / 1.80
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	103.590, 103.590, 72.132, 90.00, 90.00, 120.00
R / Rfree (%)	16.6 / 19.8

The binding sites of Calcium atom in the Crystal Structure Analysis of SERA5E From Plasmodium Falciparum (pdb code 3ch2). 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 Analysis of SERA5E From Plasmodium Falciparum, PDB code: 3ch2:

Calcium binding site 1 out of 1 in the Crystal Structure Analysis of SERA5E From Plasmodium Falciparum


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure Analysis of SERA5E From Plasmodium Falciparum within 5.0Å range: probe atom residue distance (Å) B Occ X:Ca1 b:24.7 occ:0.50 O X:HOH886 2.3 40.6 1.0 O X:HOH887 2.3 49.0 1.0 O X:HOH888 2.3 53.1 1.0 OD1 X:ASP758 2.5 40.1 1.0 OD2 X:ASP757 2.5 28.3 0.5 O X:HOH954 2.5 49.5 1.0 OD1 X:ASP757 2.7 30.7 0.5 CG X:ASP757 2.9 28.7 0.5 O X:HOH956 3.0 23.9 0.5 CG X:ASP758 3.5 34.0 1.0 NZ X:LYS737 3.8 29.2 0.5 OD2 X:ASP758 3.9 40.1 1.0 CB X:ASP757 4.3 29.9 0.5 N X:ASP758 4.3 29.5 1.0 CB X:ASP757 4.4 28.4 0.5 OD2 X:ASP757 4.4 38.1 0.5 OG1 X:THR759 4.4 30.6 1.0 CG X:ASP757 4.6 34.7 0.5 CB X:ASP758 4.7 30.0 1.0 O X:HOH1040 4.8 53.9 1.0 CE X:LYS737 4.8 30.9 0.5 N X:THR759 4.8 26.5 1.0 O X:HOH927 4.9 39.5 1.0 O X:HOH1051 4.9 45.6 1.0 CA X:ASP758 5.0 29.3 1.0

A.N.Hodder, R.L.Malby, O.B.Clarke, W.D.Fairlie, P.M.Colman, B.S.Crabb, B.J.Smith. Structural Insights Into the Protease-Like Antigen Plasmodium Falciparum SERA5 and Its Noncanonical Active-Site Serine J.Mol.Biol. V. 392 154 2009.
ISSN: ISSN 0022-2836
PubMed: 19591843
DOI: 10.1016/J.JMB.2009.07.007