Cobalt in PDB 3a4j: Arpte (K185R/D208G/N265D/T274N)

All present enzymatic activity of Arpte (K185R/D208G/N265D/T274N):
3.1.8.1;

The structure of Arpte (K185R/D208G/N265D/T274N), PDB code: 3a4j was solved by J.L.Foo, C.J.Jackson, P.D.Carr, D.L.Ollis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	30.00 / 1.25
Space group	P 31 2 1
Cell size a, b, c (Å), α, β, γ (°)	108.946, 108.946, 62.884, 90.00, 90.00, 120.00
R / Rfree (%)	12.8 / 14.5

The binding sites of Cobalt atom in the Arpte (K185R/D208G/N265D/T274N) (pdb code 3a4j). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Arpte (K185R/D208G/N265D/T274N), PDB code: 3a4j:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in the Arpte (K185R/D208G/N265D/T274N)


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Arpte (K185R/D208G/N265D/T274N) within 5.0Å range: probe atom residue distance (Å) B Occ A:Co800 b:9.0 occ:1.00 O A:HOH668 2.0 9.1 0.8 NE2 A:HIS57 2.0 9.7 1.0 NE2 A:HIS55 2.1 8.9 1.0 OQ2 A:KCX169 2.1 9.5 1.0 OD1 A:ASP301 2.2 9.2 1.0 CE1 A:HIS57 3.0 9.5 1.0 CX A:KCX169 3.0 9.1 1.0 CD2 A:HIS55 3.0 8.8 1.0 CE1 A:HIS55 3.1 8.5 1.0 CG A:ASP301 3.1 8.9 1.0 CD2 A:HIS57 3.1 9.7 1.0 OD2 A:ASP301 3.4 10.7 1.0 OQ1 A:KCX169 3.4 10.8 1.0 CO A:CO801 3.6 12.4 0.9 NZ A:KCX169 4.1 10.4 1.0 CG2 A:VAL101 4.1 10.2 1.0 ND1 A:HIS57 4.2 9.4 1.0 CE1 A:HIS230 4.2 11.4 1.0 CG A:HIS55 4.2 8.0 1.0 ND1 A:HIS55 4.2 8.9 1.0 CG A:HIS57 4.2 9.3 1.0 O A:HOH12 4.2 12.8 0.8 NE2 A:HIS230 4.4 11.8 1.0 CB A:ASP301 4.4 8.7 1.0 O A:HOH554 4.7 49.5 1.0 CA A:ASP301 4.9 8.6 1.0

Cobalt binding site 2 out of 2 in the Arpte (K185R/D208G/N265D/T274N)


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Arpte (K185R/D208G/N265D/T274N) within 5.0Å range: probe atom residue distance (Å) B Occ A:Co801 b:12.4 occ:0.90 NE2 A:HIS230 2.0 11.8 1.0 OQ1 A:KCX169 2.0 10.8 1.0 O A:HOH668 2.1 9.1 0.8 ND1 A:HIS201 2.1 13.6 1.0 O A:HOH12 2.4 12.8 0.8 CE1 A:HIS201 3.0 16.9 1.0 CE1 A:HIS230 3.0 11.4 1.0 CD2 A:HIS230 3.0 10.7 1.0 CX A:KCX169 3.1 9.1 1.0 CG A:HIS201 3.2 13.0 1.0 OQ2 A:KCX169 3.4 9.5 1.0 CO A:CO800 3.6 9.0 1.0 CB A:HIS201 3.6 11.7 1.0 NH2 A:ARG254 3.8 13.4 0.7 CE1 A:HIS55 4.1 8.5 1.0 NE2 A:HIS55 4.1 8.9 1.0 NE1 A:TRP131 4.1 12.9 1.0 NE2 A:HIS201 4.1 19.1 1.0 ND1 A:HIS230 4.1 11.1 1.0 CG A:HIS230 4.2 10.0 1.0 OD2 A:ASP301 4.2 10.7 1.0 NZ A:KCX169 4.2 10.4 1.0 CD2 A:HIS201 4.2 18.9 1.0 CA A:HIS201 4.4 10.0 1.0 CZ A:ARG254 4.5 11.3 0.7 O A:HOH420 4.6 36.2 1.0 CE A:KCX169 4.7 10.9 1.0 CD1 A:TRP131 4.7 11.9 1.0 OD1 A:ASP301 4.9 9.2 1.0 NE A:ARG254 4.9 11.3 0.7 CG A:ASP301 4.9 8.9 1.0

C.J.Jackson, J.-L.Foo, N.Tokuriki, L.Afriat, P.D.Carr, H.-K.Kim, G.Schenk, D.S.Tawfik, D.L.Ollis. Conformational Sampling, Catalysis, and Evolution of the Bacterial Phosphotriesterase Proc.Natl.Acad.Sci.Usa 2009.
ISSN: ESSN 1091-6490
PubMed: 19966226
DOI: 10.1073/PNAS.0907548106