Calcium in PDB 1xmg: Crystal Structure of Apo Methane Monooxygenase Hydroxylase From M. Capsulatus (Bath)

All present enzymatic activity of Crystal Structure of Apo Methane Monooxygenase Hydroxylase From M. Capsulatus (Bath):
1.14.13.25;

The structure of Crystal Structure of Apo Methane Monooxygenase Hydroxylase From M. Capsulatus (Bath), PDB code: 1xmg was solved by M.H.Sazinsky, M.Merkx, E.Cadieux, S.Tang, S.J.Lippard, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.77 / 2.10
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	70.352, 171.626, 220.010, 90.00, 90.00, 90.00
R / Rfree (%)	22 / 26.1

The binding sites of Calcium atom in the Crystal Structure of Apo Methane Monooxygenase Hydroxylase From M. Capsulatus (Bath) (pdb code 1xmg). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Apo Methane Monooxygenase Hydroxylase From M. Capsulatus (Bath), PDB code: 1xmg:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Apo Methane Monooxygenase Hydroxylase From M. Capsulatus (Bath)


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 Apo Methane Monooxygenase Hydroxylase From M. Capsulatus (Bath) within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca1001 b:50.5 occ:1.00 OXT A:ASN527 2.4 39.5 1.0 O A:HOH1118 2.6 37.9 1.0 O A:HOH1119 2.6 35.4 1.0 C A:ASN527 3.4 39.2 1.0 CA A:ASN527 3.8 38.4 1.0 NH1 E:ARG162 4.0 48.0 1.0 O A:PHE526 4.4 37.8 1.0 O A:ASN527 4.4 40.4 1.0 CB A:ASN527 4.8 37.0 1.0 N A:ASN527 4.9 38.6 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Apo Methane Monooxygenase Hydroxylase From M. Capsulatus (Bath)


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Apo Methane Monooxygenase Hydroxylase From M. Capsulatus (Bath) within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca1002 b:41.9 occ:1.00 OE1 C:GLU222 2.1 38.8 1.0 O C:HOH1145 2.3 26.9 1.0 O C:HOH1221 2.6 31.2 1.0 CD C:GLU222 3.3 38.8 1.0 O C:HOH1196 3.9 44.4 1.0 OE2 C:GLU222 4.1 40.1 1.0 CG C:GLU222 4.1 34.0 1.0 CB C:GLU222 4.3 30.1 1.0 CD C:LYS225 4.6 32.5 1.0 O C:HOH1251 4.7 41.7 1.0 OD2 C:ASP334 4.8 19.1 1.0 CA C:GLU222 4.9 28.1 1.0 O C:GLU222 4.9 26.3 1.0 OD1 C:ASP334 4.9 26.4 1.0 O C:HOH1039 4.9 49.5 1.0 O C:HOH1119 4.9 27.0 1.0 CG C:ASP334 5.0 23.1 1.0

M.H.Sazinsky, M.Merkx, E.Cadieux, S.Tang, S.J.Lippard. Preparation and X-Ray Structures of Metal-Free, Dicobalt and Dimanganese Forms of Soluble Methane Monooxygenase Hydroxylase From Methylococcus Capsulatus (Bath) Biochemistry V. 43 16263 2004.
ISSN: ISSN 0006-2960
PubMed: 15610020
DOI: 10.1021/BI048140Z