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Magnesium in PDB 1c1h: Crystal Structure of Bacillus Subtilis Ferrochelatase in Complex with N-Methyl Mesoporphyrin

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

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

Protein crystallography data

The structure of Crystal Structure of Bacillus Subtilis Ferrochelatase in Complex with N-Methyl Mesoporphyrin, PDB code: 1c1h 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) 20.00 / 1.90
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 49.970, 58.680, 98.050, 90.00, 90.00, 90.00
R / Rfree (%) 18.1 / 23.1

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Bacillus Subtilis Ferrochelatase in Complex with N-Methyl Mesoporphyrin (pdb code 1c1h). 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 Bacillus Subtilis Ferrochelatase in Complex with N-Methyl Mesoporphyrin, PDB code: 1c1h:

Magnesium binding site 1 out of 1 in 1c1h

Go back to Magnesium Binding Sites List in 1c1h
Magnesium binding site 1 out of 1 in the Crystal Structure 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 Bacillus Subtilis Ferrochelatase in Complex with N-Methyl Mesoporphyrin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg900

b:17.1
occ:1.00
 O A:HOH905 2.1 19.6 1.0
O A:HOH904 2.1 17.4 1.0
O A:HOH902 2.1 16.9 1.0
O A:HOH906 2.1 16.9 1.0
O A:HOH903 2.1 18.3 1.0
O A:HOH901 2.1 16.4 1.0
O A:HOH511 3.9 25.5 1.0
OD1 A:ASP268 4.0 16.1 1.0
OE1 A:GLU272 4.1 11.9 1.0
O A:HOH512 4.2 28.7 1.0
O A:HOH639 4.3 32.5 1.0
O A:HOH708 4.3 20.4 1.0
OD2 A:ASP268 4.3 13.8 1.0
OE2 A:GLU272 4.3 12.0 1.0
CG A:ASP268 4.4 14.7 1.0
O A:GLU223 4.4 12.6 1.0
CA A:SER222 4.4 8.4 1.0
O A:HOH407 4.5 10.5 1.0
NH1 A:ARG46 4.5 45.5 1.0
CD A:GLU272 4.6 12.9 1.0
C A:SER222 4.8 8.7 1.0

Reference:

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
Page generated: Tue Aug 13 02:16:56 2024

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