Magnesium in PDB 2q2n: Crystal Structure of Bacillus Subtilis Ferrochelatase in Complex with Deuteroporphyrin IX 2,4-Disulfonic Acid Dihydrochloride

All present enzymatic activity of Crystal Structure of Bacillus Subtilis Ferrochelatase in Complex with Deuteroporphyrin IX 2,4-Disulfonic Acid Dihydrochloride:
4.99.1.1;

The structure of Crystal Structure of Bacillus Subtilis Ferrochelatase in Complex with Deuteroporphyrin IX 2,4-Disulfonic Acid Dihydrochloride, PDB code: 2q2n was solved by T.Karlberg, O.H.Thorvaldsen, S.Al-Karadaghi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.55 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	48.300, 49.900, 118.200, 90.00, 90.00, 90.00
R / Rfree (%)	19.2 / 25

The binding sites of Magnesium atom in the Crystal Structure of Bacillus Subtilis Ferrochelatase in Complex with Deuteroporphyrin IX 2,4-Disulfonic Acid Dihydrochloride (pdb code 2q2n). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Bacillus Subtilis Ferrochelatase in Complex with Deuteroporphyrin IX 2,4-Disulfonic Acid Dihydrochloride, PDB code: 2q2n:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Bacillus Subtilis Ferrochelatase in Complex with Deuteroporphyrin IX 2,4-Disulfonic Acid Dihydrochloride


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of Bacillus Subtilis Ferrochelatase in Complex with Deuteroporphyrin IX 2,4-Disulfonic Acid Dihydrochloride within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1000 b:27.3 occ:1.00 O A:HOH9002 2.2 25.3 1.0 O A:HOH9005 2.2 27.4 1.0 O A:HOH9004 2.2 27.9 1.0 O A:HOH9006 2.2 25.1 1.0 O A:HOH9007 2.2 25.9 1.0 O A:HOH9003 2.2 25.6 1.0 O A:HOH9240 4.0 35.5 1.0 O A:HOH9093 4.1 41.8 1.0 OE1 A:GLU272 4.2 24.0 1.0 OE2 A:GLU272 4.2 23.1 1.0 OD2 A:ASP268 4.2 23.2 1.0 OD1 A:ASP268 4.3 24.3 1.0 O A:HOH9030 4.4 21.1 1.0 CA A:SER222 4.5 21.5 1.0 O A:GLU223 4.5 22.8 1.0 CG A:ASP268 4.5 23.1 1.0 NH1 A:ARG46 4.5 27.8 1.0 CD A:GLU272 4.6 22.7 1.0 C A:SER222 4.8 21.6 1.0 O A:HOH9110 4.9 30.1 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Bacillus Subtilis Ferrochelatase in Complex with Deuteroporphyrin IX 2,4-Disulfonic Acid Dihydrochloride


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Bacillus Subtilis Ferrochelatase in Complex with Deuteroporphyrin IX 2,4-Disulfonic Acid Dihydrochloride within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg2000 b:37.8 occ:1.00 O A:HOH9010 2.2 36.2 1.0 O A:HOH9011 2.2 36.7 1.0 O A:HOH9013 2.2 36.8 1.0 O A:HOH9009 2.2 36.6 1.0 O A:HOH9012 2.2 36.5 1.0 O A:HOH9008 2.2 36.9 1.0 O A:HOH9262 4.1 31.2 1.0 O A:THR226 4.1 29.0 1.0 O A:PRO227 4.2 30.9 1.0 O A:ASP228 4.2 31.2 1.0 O A:HOH9106 4.3 26.0 1.0 C A:ASP228 4.5 31.4 1.0 N A:PRO229 4.5 31.1 1.0 CA A:PRO229 4.6 31.3 1.0 C A:PRO227 4.7 30.6 1.0 O A:HOH9268 4.9 34.1 1.0 CB A:PRO229 4.9 31.4 1.0

T.Karlberg, M.D.Hansson, R.K.Yengo, R.Johansson, O.H.Thorvaldsen, G.C.Ferreira, M.Hansson, S.Al-Karadaghi. Porphyrin Binding and Distortion and Substrate Specificity in the Ferrochelatase Reaction: the Role of Active Site Residues J.Mol.Biol. V. 378 1074 2008.
ISSN: ISSN 0022-2836
PubMed: 18423489
DOI: 10.1016/J.JMB.2008.03.040