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Magnesium in PDB 2hk6: Crystal Structure of B. Subtilis Ferrochelatase with Iron Bound at the Active Site

Enzymatic activity of Crystal Structure of B. Subtilis Ferrochelatase with Iron Bound at the Active Site

All present enzymatic activity of Crystal Structure of B. Subtilis Ferrochelatase with Iron Bound at the Active Site:
4.99.1.1;

Protein crystallography data

The structure of Crystal Structure of B. Subtilis Ferrochelatase with Iron Bound at the Active Site, PDB code: 2hk6 was solved by S.Al-Karadaghi, T.Karlberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.64 / 1.71
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 48.650, 49.980, 118.850, 90.00, 90.00, 90.00
R / Rfree (%) 17.6 / 22

Other elements in 2hk6:

The structure of Crystal Structure of B. Subtilis Ferrochelatase with Iron Bound at the Active Site also contains other interesting chemical elements:

Iron (Fe) 4 atoms

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of B. Subtilis Ferrochelatase with Iron Bound at the Active Site (pdb code 2hk6). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 3 binding sites of Magnesium where determined in the Crystal Structure of B. Subtilis Ferrochelatase with Iron Bound at the Active Site, PDB code: 2hk6:
Jump to Magnesium binding site number: 1; 2; 3;

Magnesium binding site 1 out of 3 in 2hk6

Go back to Magnesium Binding Sites List in 2hk6
Magnesium binding site 1 out of 3 in the Crystal Structure of B. Subtilis Ferrochelatase with Iron Bound at the Active Site


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 B. Subtilis Ferrochelatase with Iron Bound at the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg400

b:20.3
occ:1.00
O A:HOH974 2.2 23.4 1.0
O A:HOH969 2.2 20.0 1.0
O A:HOH972 2.2 21.7 1.0
O A:HOH973 2.2 21.6 1.0
O A:HOH971 2.2 20.9 1.0
O A:HOH970 2.2 21.9 1.0
OD2 A:ASP268 4.1 17.6 1.0
OE1 A:GLU272 4.2 13.7 1.0
OE2 A:GLU272 4.3 15.3 1.0
OD1 A:ASP268 4.4 18.8 1.0
CA A:SER222 4.4 12.7 1.0
CG A:ASP268 4.5 15.7 1.0
O A:HOH627 4.5 12.9 1.0
O A:GLU223 4.6 19.4 1.0
NH1 A:ARG46 4.7 25.8 1.0
CD A:GLU272 4.7 14.4 1.0
O A:HOH854 4.8 26.9 1.0
C A:SER222 4.9 14.7 1.0

Magnesium binding site 2 out of 3 in 2hk6

Go back to Magnesium Binding Sites List in 2hk6
Magnesium binding site 2 out of 3 in the Crystal Structure of B. Subtilis Ferrochelatase with Iron Bound at the Active Site


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 B. Subtilis Ferrochelatase with Iron Bound at the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg401

b:20.9
occ:1.00
O A:HOH979 2.2 19.2 1.0
O A:HOH976 2.2 20.9 1.0
O A:HOH977 2.2 21.3 1.0
O A:HOH980 2.2 22.0 1.0
O A:HOH975 2.2 22.1 1.0
O A:HOH978 2.2 21.1 1.0
OG A:SER146 3.7 10.5 1.0
OD2 A:ASP149 4.2 15.7 1.0
OD1 A:ASP149 4.3 14.2 1.0
O A:HOH818 4.3 25.1 1.0
O A:HOH611 4.4 16.9 1.0
O A:HOH864 4.5 26.3 1.0
O A:SER146 4.5 9.2 1.0
O A:HOH721 4.6 25.2 1.0
O A:HOH601 4.7 4.7 1.0
CG A:ASP149 4.7 13.1 1.0
O A:HOH700 4.9 4.2 1.0
O A:HOH667 5.0 17.6 1.0

Magnesium binding site 3 out of 3 in 2hk6

Go back to Magnesium Binding Sites List in 2hk6
Magnesium binding site 3 out of 3 in the Crystal Structure of B. Subtilis Ferrochelatase with Iron Bound at the Active Site


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 B. Subtilis Ferrochelatase with Iron Bound at the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg402

b:20.3
occ:1.00
OE2 A:GLU20 2.1 16.4 1.0
O A:HOH985 2.1 22.9 1.0
O A:HOH983 2.2 23.4 1.0
O A:HOH982 2.2 22.9 1.0
O A:HOH981 2.2 24.9 1.0
O A:HOH984 2.2 27.7 1.0
CD A:GLU20 3.1 15.4 1.0
OE1 A:GLU20 3.3 11.6 1.0
O A:HOH829 4.4 31.0 1.0
CG A:GLU20 4.4 11.0 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 23:53:47 2024

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