Calcium in PDB 1o7l: Molybdate-Activated Form of Mode From Escherichia Coli

The structure of Molybdate-Activated Form of Mode From Escherichia Coli, PDB code: 1o7l was solved by A.W.Schuttelkopf, W.N.Hunter, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 2.75
Space group	P 43
Cell size a, b, c (Å), α, β, γ (°)	78.831, 78.831, 195.099, 90.00, 90.00, 90.00
R / Rfree (%)	20.7 / 25.4

The structure of Molybdate-Activated Form of Mode From Escherichia Coli also contains other interesting chemical elements:

Molybdenum	(Mo)	5 atoms
Chlorine	(Cl)	1 atom

The binding sites of Calcium atom in the Molybdate-Activated Form of Mode From Escherichia Coli (pdb code 1o7l). 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 Molybdate-Activated Form of Mode From Escherichia Coli, PDB code: 1o7l:

Calcium binding site 1 out of 1 in the Molybdate-Activated Form of Mode From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Molybdate-Activated Form of Mode From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca1265 b:44.1 occ:1.00 O3 D:MOO1264 2.8 37.5 1.0 OD2 D:ASP141 2.9 33.5 1.0 O D:GLN144 3.0 22.1 1.0 O D:HOH2004 3.1 19.1 1.0 OE1 C:GLU215 3.5 48.4 1.0 CG D:ASP141 3.9 30.7 1.0 ND1 D:HIS146 4.0 30.2 1.0 C D:GLN144 4.1 22.1 1.0 CE1 D:HIS146 4.1 30.7 1.0 MO D:MOO1264 4.2 34.0 1.0 CE1 B:HIS140 4.3 39.0 1.0 CB D:ASP141 4.3 30.3 1.0 O1 D:MOO1264 4.4 38.6 1.0 OE1 D:GLN144 4.5 26.0 1.0 CB D:GLN144 4.6 20.2 1.0 CD C:GLU215 4.6 46.1 1.0 ND1 B:HIS140 4.7 37.2 1.0 O2 D:MOO1264 4.7 42.9 1.0 CA D:GLN144 4.8 22.0 1.0 OD1 D:ASP141 4.9 29.1 1.0 N D:GLN145 5.0 23.4 1.0 CG D:GLN144 5.0 20.7 1.0 OD2 D:ASP139 5.0 27.7 1.0

A.W.Schuttelkopf, D.H.Boxer, W.N.Hunter. Crystal Structure of Activated Mode Reveals Conformational Changes Involving Both Oxyanion and Dna-Binding Domains J.Mol.Biol. V. 326 761 2003.
ISSN: ISSN 0022-2836
PubMed: 12581638
DOI: 10.1016/S0022-2836(02)01358-X