Calcium in PDB 8fjd: Structure of Chlorophyllase From Triticum Aestivum

The structure of Structure of Chlorophyllase From Triticum Aestivum, PDB code: 8fjd was solved by D.Boggs, M.Jo, J.Bridwell-Rabb, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.13 / 4.46
Space group	P 65 2 2
Cell size a, b, c (Å), α, β, γ (°)	197.52, 197.52, 96.83, 90, 90, 120
R / Rfree (%)	26.6 / 27.8

The binding sites of Calcium atom in the Structure of Chlorophyllase From Triticum Aestivum (pdb code 8fjd). 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 Structure of Chlorophyllase From Triticum Aestivum, PDB code: 8fjd:

Calcium binding site 1 out of 1 in the Structure of Chlorophyllase From Triticum Aestivum


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Structure of Chlorophyllase From Triticum Aestivum within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca401 b:73.7 occ:1.00 O A:HOH501 2.3 101.6 1.0 OD2 A:ASP255 2.5 111.1 1.0 O B:HOH401 2.5 89.2 1.0 O B:HOH402 2.6 114.3 1.0 O A:HOH502 2.7 98.3 1.0 OD2 B:ASP255 2.7 119.7 1.0 NE2 A:HIS76 2.8 102.2 1.0 CG B:ASP255 2.9 116.9 1.0 CE1 B:HIS76 3.0 97.2 1.0 CG A:ASP255 3.0 111.5 1.0 OD1 B:ASP255 3.0 113.3 1.0 NE2 B:HIS76 3.0 93.9 1.0 OD1 A:ASP255 3.1 109.7 1.0 OE1 A:GLU79 3.2 121.8 1.0 CD2 A:HIS76 3.6 99.7 1.0 CE1 A:HIS76 3.6 109.9 1.0 CB B:ASP255 4.0 115.4 1.0 ND1 B:HIS76 4.1 109.2 1.0 OD2 A:ASP253 4.2 104.3 1.0 CB A:ASP255 4.2 112.2 1.0 CD2 B:HIS76 4.3 102.8 1.0 CD A:GLU79 4.3 113.7 1.0 OE1 B:GLU79 4.4 113.7 1.0 O A:HIS76 4.6 95.8 1.0 ND1 A:HIS76 4.6 108.0 1.0 CG A:HIS76 4.7 99.4 1.0 CD B:GLU79 4.7 115.6 1.0 OD2 B:ASP253 4.7 112.9 1.0 CB A:GLU79 4.7 100.7 1.0 CG B:HIS76 4.8 107.3 1.0 O B:HIS76 5.0 109.1 1.0

M.Jo, M.Knapp, D.Boggs, M.Brimberry, P.Donnan, J.Bridwell-Rabb. A Structure-Function Analysis of Chlorophyllase Reveals A Mechanism For Activity Regulation Dependent on Disulfide Bonds J.Biol.Chem. 2023.
ISSN: ESSN 1083-351X