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Cobalt in PDB 3wml: Structure of Phosphotriesterase Mutant (S308L/Y309A) From Agrobacterium Radiobacter

Enzymatic activity of Structure of Phosphotriesterase Mutant (S308L/Y309A) From Agrobacterium Radiobacter

All present enzymatic activity of Structure of Phosphotriesterase Mutant (S308L/Y309A) From Agrobacterium Radiobacter:
3.1.8.1;

Protein crystallography data

The structure of Structure of Phosphotriesterase Mutant (S308L/Y309A) From Agrobacterium Radiobacter, PDB code: 3wml was solved by C.J.Jackson, P.D.Carr, E.Sugrue, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 29.36 / 1.99
Space group P 31 2 1
Cell size a, b, c (Å), α, β, γ (°) 108.996, 108.996, 61.774, 90.00, 90.00, 120.00
R / Rfree (%) 15.7 / 18.7

Other elements in 3wml:

The structure of Structure of Phosphotriesterase Mutant (S308L/Y309A) From Agrobacterium Radiobacter also contains other interesting chemical elements:

Iron (Fe) 1 atom

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Structure of Phosphotriesterase Mutant (S308L/Y309A) From Agrobacterium Radiobacter (pdb code 3wml). 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 Structure of Phosphotriesterase Mutant (S308L/Y309A) From Agrobacterium Radiobacter, PDB code: 3wml:

Cobalt binding site 1 out of 1 in 3wml

Go back to Cobalt Binding Sites List in 3wml
Cobalt binding site 1 out of 1 in the Structure of Phosphotriesterase Mutant (S308L/Y309A) From Agrobacterium Radiobacter


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Structure of Phosphotriesterase Mutant (S308L/Y309A) From Agrobacterium Radiobacter within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co402

b:14.9
occ:0.90
 OQ2 A:KCX169 2.1 18.0 1.0
CE1 A:HIS230 2.1 15.2 1.0
O A:HOH615 2.1 22.0 1.0
ND1 A:HIS201 2.1 14.0 1.0
O A:HOH614 2.2 21.1 1.0
OQ1 A:KCX169 2.3 15.7 1.0
CX A:KCX169 2.6 21.3 1.0
NE2 A:HIS230 3.0 17.8 1.0
CE1 A:HIS201 3.0 14.4 1.0
ND1 A:HIS230 3.1 18.8 1.0
CG A:HIS201 3.2 14.1 1.0
CB A:HIS201 3.6 13.8 1.0
FE A:FE2401 3.7 11.8 0.9
NZ A:KCX169 3.9 22.8 1.0
NE1 A:TRP131 4.0 20.7 1.0
NE2 A:HIS201 4.2 14.9 1.0
CD2 A:HIS230 4.2 13.8 1.0
NE2 A:HIS55 4.2 14.2 1.0
CG A:HIS230 4.3 17.5 1.0
CD2 A:HIS201 4.3 14.6 1.0
CE1 A:HIS55 4.3 12.3 1.0
OD2 A:ASP301 4.4 14.0 1.0
CA A:HIS201 4.5 13.0 1.0
CD1 A:TRP131 4.8 21.8 1.0
CE A:KCX169 4.8 17.8 1.0
CE2 A:TRP131 5.0 18.1 1.0
O A:HOH601 5.0 25.4 1.0

Reference:

T.Naqvi, A.C.Warden, N.French, E.Sugrue, P.D.Carr, C.J.Jackson, C.Scott. A 5000-Fold Increase in the Specificity of A Bacterial Phosphotriesterase For Malathion Through Combinatorial Active Site Mutagenesis Plos One V. 9 94177 2014.
ISSN: ESSN 1932-6203
PubMed: 24721933
DOI: 10.1371/JOURNAL.PONE.0094177
Page generated: Tue Jul 30 16:54:47 2024

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