Magnesium in PDB 1doz: Crystal Structure of Ferrochelatase

All present enzymatic activity of Crystal Structure of Ferrochelatase:
4.99.1.1;

The structure of Crystal Structure of Ferrochelatase, PDB code: 1doz was solved by D.Lecerof, M.Fodje, A.Hansson, M.Hansson, S.Al-Karadaghi, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	14.91 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	48.510, 49.970, 119.240, 90.00, 90.00, 90.00
R / Rfree (%)	18.3 / 21.6

The binding sites of Magnesium atom in the Crystal Structure of Ferrochelatase (pdb code 1doz). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of Ferrochelatase, PDB code: 1doz:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in the Crystal Structure of Ferrochelatase


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 Ferrochelatase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg900 b:21.4 occ:1.00 O A:HOH1206 2.0 21.4 1.0 O A:HOH1202 2.1 21.4 1.0 O A:HOH1204 2.1 21.4 1.0 O A:HOH1205 2.1 21.4 1.0 O A:HOH1207 2.1 21.4 1.0 O A:HOH1203 2.2 21.4 1.0 O A:HOH1152 4.0 35.8 1.0 OE2 A:GLU272 4.1 14.7 1.0 OE1 A:GLU272 4.1 13.7 1.0 OD1 A:ASP268 4.1 17.2 1.0 OD2 A:ASP268 4.2 15.2 1.0 CG A:ASP268 4.4 14.6 1.0 O A:HOH995 4.4 20.7 1.0 CD A:GLU272 4.5 14.6 1.0 NH1 A:ARG46 4.5 22.1 1.0 CA A:SER222 4.5 12.3 1.0 O A:GLU223 4.6 13.8 1.0 O A:HOH924 4.6 10.2 1.0 O A:HOH1056 4.8 21.5 1.0 O A:HOH1186 4.9 35.0 1.0 O A:HOH1139 4.9 33.6 1.0 C A:SER222 4.9 12.6 1.0

Magnesium binding site 2 out of 3 in the Crystal Structure of Ferrochelatase


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 Ferrochelatase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg901 b:21.4 occ:1.00 O A:HOH1212 2.0 21.4 1.0 O A:HOH1208 2.1 21.4 1.0 O A:HOH1210 2.1 21.4 1.0 O A:HOH1211 2.1 21.4 1.0 O A:HOH1213 2.1 21.4 1.0 O A:HOH1209 2.2 21.4 1.0 OG A:SER146 3.8 12.7 1.0 OD2 A:ASP149 4.1 18.2 1.0 OD1 A:ASP149 4.3 12.1 1.0 O A:HOH958 4.4 14.1 1.0 O A:HOH1126 4.4 25.5 1.0 O A:HOH1143 4.5 23.6 1.0 O A:SER146 4.6 9.5 1.0 CG A:ASP149 4.7 14.8 1.0 O A:HOH1201 4.7 2.0 1.0

Magnesium binding site 3 out of 3 in the Crystal Structure of Ferrochelatase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of Ferrochelatase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg902 b:21.4 occ:1.00 O A:HOH1218 2.0 21.4 1.0 O A:HOH1214 2.1 21.4 1.0 O A:HOH1216 2.1 21.4 1.0 O A:HOH1217 2.1 21.4 1.0 O A:HOH1215 2.2 21.4 1.0 OE2 A:GLU20 2.3 13.3 1.0 CD A:GLU20 3.2 13.2 1.0 OE1 A:GLU20 3.5 13.6 1.0 O A:HOH1156 4.0 35.2 1.0 O A:HOH1127 4.3 23.2 1.0 CG A:GLU20 4.6 11.0 1.0

D.Lecerof, M.Fodje, A.Hansson, M.Hansson, S.Al-Karadaghi. Structural and Mechanistic Basis of Porphyrin Metallation By Ferrochelatase. J.Mol.Biol. V. 297 221 2000.
ISSN: ISSN 0022-2836
PubMed: 10704318
DOI: 10.1006/JMBI.2000.3569