Magnesium in PDB 2h1v: Crystal Structure of the LYS87ALA Mutant Variant of Bacillus Subtilis Ferrochelatase

All present enzymatic activity of Crystal Structure of the LYS87ALA Mutant Variant of Bacillus Subtilis Ferrochelatase:
4.99.1.1;

The structure of Crystal Structure of the LYS87ALA Mutant Variant of Bacillus Subtilis Ferrochelatase, PDB code: 2h1v 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)	25.00 / 1.20
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	47.700, 49.400, 117.200, 90.00, 90.00, 90.00
R / Rfree (%)	12.3 / 17.3

The binding sites of Magnesium atom in the Crystal Structure of the LYS87ALA Mutant Variant of Bacillus Subtilis Ferrochelatase (pdb code 2h1v). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Crystal Structure of the LYS87ALA Mutant Variant of Bacillus Subtilis Ferrochelatase, PDB code: 2h1v:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Crystal Structure of the LYS87ALA 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 LYS87ALA Mutant Variant of Bacillus Subtilis Ferrochelatase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg400 b:25.2 occ:1.00 O A:HOH974 1.9 40.6 1.0 O A:HOH970 2.0 24.5 1.0 O A:HOH971 2.1 32.4 1.0 O A:HOH969 2.1 38.5 1.0 O A:HOH972 2.1 40.0 1.0 O A:HOH973 2.4 25.7 1.0 OE1 A:GLU272 4.1 14.1 1.0 O A:HOH847 4.2 34.9 1.0 NH2 A:ARG46 4.2 41.1 1.0 OD2 A:ASP268 4.2 19.7 1.0 NH1 A:ARG46 4.3 47.5 1.0 OE2 A:GLU272 4.3 14.2 1.0 O A:HOH572 4.4 11.5 1.0 OD1 A:ASP268 4.4 24.4 1.0 CA A:SER222 4.4 14.6 1.0 O A:GLU223 4.5 22.3 1.0 CG A:ASP268 4.5 15.4 1.0 CD A:GLU272 4.6 10.5 1.0 CZ A:ARG46 4.7 28.1 1.0 C A:SER222 4.8 16.0 1.0 N A:SER222 4.9 10.2 1.0

Magnesium binding site 2 out of 4 in the Crystal Structure of the LYS87ALA 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 2 of Crystal Structure of the LYS87ALA Mutant Variant of Bacillus Subtilis Ferrochelatase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:24.2 occ:0.95 O A:HOH979 2.0 43.2 0.9 O A:HOH975 2.0 25.3 0.9 O A:HOH980 2.0 19.2 0.9 O A:HOH976 2.0 55.2 0.9 O A:HOH977 2.1 30.4 0.9 O A:HOH978 2.2 31.4 0.9 O A:HOH637 3.7 19.2 1.0 NZ A:LYS18 3.8 16.1 1.0 O A:HOH744 4.0 20.2 1.0 O A:HOH671 4.1 25.3 1.0 OE1 A:GLU90 4.2 21.3 0.4 OD1 A:ASP21 4.3 10.9 1.0 OD2 A:ASP21 4.8 9.2 1.0 O A:HOH948 4.8 39.6 1.0 CE A:LYS18 5.0 15.6 1.0 CG A:ASP21 5.0 7.6 1.0 OE2 A:GLU20 5.0 13.1 1.0

Magnesium binding site 3 out of 4 in the Crystal Structure of the LYS87ALA 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 3 of Crystal Structure of the LYS87ALA Mutant Variant of Bacillus Subtilis Ferrochelatase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:24.4 occ:0.70 O A:HOH982 1.9 34.7 0.7 O A:HOH984 2.1 23.6 0.7 O A:HOH985 2.2 33.9 0.7 O A:HOH983 2.2 39.9 0.7 O A:HOH981 2.2 12.6 0.7 O A:HOH986 2.6 70.3 0.7 OG A:SER146 3.9 11.8 1.0 O A:HOH648 4.3 15.8 1.0 O A:HOH935 4.3 33.6 1.0 O A:SER146 4.3 6.8 1.0 OD1 A:ASP149 4.4 11.5 1.0 OD2 A:ASP149 4.5 24.9 1.0 O A:HOH501 4.7 5.8 1.0 O A:HOH642 4.8 18.3 1.0 CG A:ASP149 4.9 13.7 1.0 O A:HOH502 4.9 6.5 1.0

Magnesium binding site 4 out of 4 in the Crystal Structure of the LYS87ALA 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 4 of Crystal Structure of the LYS87ALA Mutant Variant of Bacillus Subtilis Ferrochelatase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg403 b:23.2 occ:0.85 O A:HOH991 1.9 48.4 0.8 O A:HOH992 2.0 22.8 0.8 O A:HOH989 2.0 16.2 0.8 O A:HOH990 2.1 21.6 0.8 O A:HOH988 2.2 19.6 0.8 O A:HOH987 2.6 35.8 0.8 O A:HOH723 4.0 18.5 1.0 O A:HOH763 4.0 26.0 1.0 OE2 A:GLU132 4.0 13.4 1.0 OE1 A:GLU132 4.1 12.0 1.0 CD A:GLU132 4.5 11.0 1.0 O A:HOH615 4.5 14.7 1.0 O A:HOH808 4.7 24.3 1.0 CB A:GLU94 4.8 7.2 1.0

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