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Magnesium in PDB 2h1w: Crystal Structure of the HIS183ALA Mutant Variant of Bacillus Subtilis Ferrochelatase

Enzymatic activity of Crystal Structure of the HIS183ALA Mutant Variant of Bacillus Subtilis Ferrochelatase

All present enzymatic activity of Crystal Structure of the HIS183ALA Mutant Variant of Bacillus Subtilis Ferrochelatase:
4.99.1.1;

Protein crystallography data

The structure of Crystal Structure of the HIS183ALA Mutant Variant of Bacillus Subtilis Ferrochelatase, PDB code: 2h1w was solved by M.D.Hansson, T.Karlberg, M.Arys Rahardja, S.Al-Karadaghi, M.Hansson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.30 / 2.60
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 47.940, 49.720, 116.540, 90.00, 90.00, 90.00
R / Rfree (%) 21.8 / 25.9

Other elements in 2h1w:

The structure of Crystal Structure of the HIS183ALA Mutant Variant of Bacillus Subtilis Ferrochelatase also contains other interesting chemical elements:

Iron (Fe) 1 atom

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the HIS183ALA Mutant Variant of Bacillus Subtilis Ferrochelatase (pdb code 2h1w). 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 Mutant Variant of Bacillus Subtilis Ferrochelatase, PDB code: 2h1w:

Magnesium binding site 1 out of 1 in 2h1w

Go back to Magnesium Binding Sites List in 2h1w
Magnesium binding site 1 out of 1 in the Crystal Structure of the HIS183ALA Mutant Variant of Bacillus Subtilis 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 the HIS183ALA Mutant Variant of Bacillus Subtilis Ferrochelatase within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg600

b:64.3
occ:1.00
 O A:HOH412 2.0 63.9 1.0
O A:HOH411 2.1 63.8 1.0
O A:HOH409 2.1 63.4 1.0
O A:HOH413 2.1 63.4 1.0
O A:HOH410 2.1 63.8 1.0
O A:HOH408 2.1 63.6 1.0
OD1 A:ASP268 4.4 69.0 1.0
OE1 A:GLU272 4.5 0.6 1.0
OE2 A:GLU272 4.6 0.6 1.0
OE1 A:GLN236 4.7 44.4 1.0
O A:GLU223 4.8 36.8 1.0
CA A:SER222 4.8 42.9 1.0
N A:GLU223 4.9 36.4 1.0
N A:SER222 4.9 39.5 1.0
CD A:GLU272 5.0 99.9 1.0

Reference:

M.D.Hansson, T.Karlberg, M.A.Rahardja, S.Al-Karadaghi, M.Hansson. Amino Acid Residues HIS183 and GLU264 in Bacillus Subtilis Ferrochelatase Direct and Facilitate the Insertion of Metal Ion Into Protoporphyrin IX Biochemistry V. 46 87 2007.
ISSN: ISSN 0006-2960
PubMed: 17198378
DOI: 10.1021/BI061760A
Page generated: Tue Aug 13 23:41:55 2024

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