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Cobalt in PDB 3m4z: Crystal Structure of B. Subtilis Ferrochelatase with Cobalt Bound at the Active Site

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

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

Protein crystallography data

The structure of Crystal Structure of B. Subtilis Ferrochelatase with Cobalt Bound at the Active Site, PDB code: 3m4z was solved by C.A.G.Soderberg, M.D.Hansson, R.Sreekanth, S.Al-Karadaghi, M.Hansson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.94
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 48.410, 49.900, 118.080, 90.00, 90.00, 90.00
R / Rfree (%) 16.8 / 19.9

Other elements in 3m4z:

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

Magnesium (Mg) 3 atoms
Chlorine (Cl) 2 atoms

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Crystal Structure of B. Subtilis Ferrochelatase with Cobalt Bound at the Active Site (pdb code 3m4z). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total only one binding site of Cobalt was determined in the Crystal Structure of B. Subtilis Ferrochelatase with Cobalt Bound at the Active Site, PDB code: 3m4z:

Cobalt binding site 1 out of 1 in 3m4z

Go back to Cobalt Binding Sites List in 3m4z
Cobalt binding site 1 out of 1 in the Crystal Structure of B. Subtilis Ferrochelatase with Cobalt Bound at the Active Site


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Crystal Structure of B. Subtilis Ferrochelatase with Cobalt Bound at the Active Site within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co310

b:18.3
occ:0.60
 O A:HOH532 1.6 30.7 1.0
O A:HOH514 1.8 26.3 1.0
OE2 A:GLU263 2.0 16.8 0.5
O A:HOH531 2.1 32.0 1.0
NE2 A:HIS182 2.1 16.5 1.0
O A:HOH460 2.5 22.9 1.0
CD2 A:HIS182 3.0 15.7 1.0
CE1 A:HIS182 3.1 16.3 1.0
CD A:GLU263 3.1 16.1 0.5
OE1 A:GLU263 3.5 14.1 0.5
O A:SER221 4.0 19.4 1.0
OH A:TYR12 4.0 28.8 1.0
O A:HOH529 4.0 37.7 1.0
OE2 A:GLU263 4.1 18.3 0.5
ND1 A:HIS182 4.2 15.6 1.0
CG A:HIS182 4.2 14.3 1.0
CZ A:TYR12 4.4 25.0 1.0
CG A:GLU263 4.4 15.6 0.5
CG A:GLU263 4.5 15.1 0.5
CB A:SER221 4.5 16.6 1.0
CD A:GLU263 4.6 17.4 0.5
CE2 A:TYR12 4.7 24.9 1.0
O A:HOH490 5.0 44.4 1.0

Reference:

M.D.Hansson, T.Karlberg, C.A.G.Soderberg, R.Sreekanth, M.J.Warren, S.Al-Karadaghi, S.E.J.Rigby, M.Hansson. Bacterial Ferrochelatase Goes Human: TYR13 Determines the Apparent Metal Specificity of Bacillus Subtilis Ferrochelatase To Be Published.
Page generated: Tue Jul 30 16:18:32 2024

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