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Magnesium in PDB 2q2o: Crystal Structure of H183C Bacillus Subtilis Ferrochelatase in Complex with Deuteroporphyrin IX 2,4-Disulfonic Acid Dihydrochloride

Enzymatic activity of Crystal Structure of H183C Bacillus Subtilis Ferrochelatase in Complex with Deuteroporphyrin IX 2,4-Disulfonic Acid Dihydrochloride

All present enzymatic activity of Crystal Structure of H183C Bacillus Subtilis Ferrochelatase in Complex with Deuteroporphyrin IX 2,4-Disulfonic Acid Dihydrochloride:
4.99.1.1;

Protein crystallography data

The structure of Crystal Structure of H183C Bacillus Subtilis Ferrochelatase in Complex with Deuteroporphyrin IX 2,4-Disulfonic Acid Dihydrochloride, PDB code: 2q2o 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) 45.69 / 2.10
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.600, 49.700, 116.300, 90.00, 90.00, 90.00
R / Rfree (%) 18.5 / 21.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of H183C Bacillus Subtilis Ferrochelatase in Complex with Deuteroporphyrin IX 2,4-Disulfonic Acid Dihydrochloride (pdb code 2q2o). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of H183C Bacillus Subtilis Ferrochelatase in Complex with Deuteroporphyrin IX 2,4-Disulfonic Acid Dihydrochloride, PDB code: 2q2o:

Magnesium binding site 1 out of 1 in 2q2o

Go back to Magnesium Binding Sites List in 2q2o
Magnesium binding site 1 out of 1 in the Crystal Structure of H183C 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 H183C 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:34.6
occ:1.00
 O A:HOH9002 2.1 30.5 1.0
O A:HOH9007 2.2 31.3 1.0
O A:HOH9004 2.2 31.9 1.0
O A:HOH9003 2.2 31.4 1.0
O A:HOH9006 2.2 29.5 1.0
O A:HOH9005 2.2 30.7 1.0
OE2 A:GLU272 4.1 29.4 1.0
OE1 A:GLU272 4.2 32.2 1.0
OD1 A:ASP268 4.3 31.6 1.0
OD2 A:ASP268 4.3 32.4 1.0
CG A:ASP268 4.5 32.3 1.0
CD A:GLU272 4.6 28.5 1.0
O A:HOH9057 4.6 15.0 1.0
NH1 A:ARG46 4.6 50.7 1.0
O A:GLU223 4.6 33.4 1.0
CA A:SER222 4.7 29.5 1.0
O A:HOH9129 4.9 36.0 1.0
O A:HOH9024 4.9 22.0 1.0

Reference:

T.Karlberg, M.D.Hansson, R.K.Yengo, R.Johansson, H.O.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
Page generated: Wed Aug 14 02:34:29 2024

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