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Magnesium in PDB 2q3j: Crystal Structure of the HIS183ALA Variant of Bacillus Subtilis Ferrochelatase in Complex with N-Methyl Mesoporphyrin

Enzymatic activity of Crystal Structure of the HIS183ALA Variant of Bacillus Subtilis Ferrochelatase in Complex with N-Methyl Mesoporphyrin

All present enzymatic activity of Crystal Structure of the HIS183ALA Variant of Bacillus Subtilis Ferrochelatase in Complex with N-Methyl Mesoporphyrin:
4.99.1.1;

Protein crystallography data

The structure of Crystal Structure of the HIS183ALA Variant of Bacillus Subtilis Ferrochelatase in Complex with N-Methyl Mesoporphyrin, PDB code: 2q3j 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) 20.00 / 2.39
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 49.780, 58.570, 97.830, 90.00, 90.00, 90.00
R / Rfree (%) 18.3 / 22.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the HIS183ALA Variant of Bacillus Subtilis Ferrochelatase in Complex with N-Methyl Mesoporphyrin (pdb code 2q3j). 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 the HIS183ALA Variant of Bacillus Subtilis Ferrochelatase in Complex with N-Methyl Mesoporphyrin, PDB code: 2q3j:

Magnesium binding site 1 out of 1 in 2q3j

Go back to Magnesium Binding Sites List in 2q3j
Magnesium binding site 1 out of 1 in the Crystal Structure of the HIS183ALA Variant of Bacillus Subtilis Ferrochelatase in Complex with N-Methyl Mesoporphyrin


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 the HIS183ALA Variant of Bacillus Subtilis Ferrochelatase in Complex with N-Methyl Mesoporphyrin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1000

b:27.4
occ:1.00
 O A:HOH1002 2.1 24.5 1.0
O A:HOH1004 2.1 23.5 1.0
O A:HOH1003 2.1 25.4 1.0
O A:HOH1001 2.1 25.4 1.0
O A:HOH1006 2.1 26.1 1.0
O A:HOH1005 2.1 24.9 1.0
OD1 A:ASP268 4.0 22.3 1.0
O A:HOH1146 4.2 28.8 1.0
OE1 A:GLU272 4.2 22.4 1.0
O A:HOH1127 4.4 38.2 1.0
OE2 A:GLU272 4.4 22.6 1.0
OD2 A:ASP268 4.4 22.6 1.0
CG A:ASP268 4.5 20.3 1.0
O A:HOH1073 4.5 19.7 1.0
O A:GLU223 4.6 19.9 1.0
CA A:SER222 4.6 12.2 1.0
CD A:GLU272 4.7 23.9 1.0
NH1 A:ARG46 4.8 28.4 1.0

Reference:

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
Page generated: Wed Aug 14 02:35:18 2024

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