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Cobalt in PDB 8sfb: Crystal Structure of the Engineered Ssopox Variant IVA4

Enzymatic activity of Crystal Structure of the Engineered Ssopox Variant IVA4

All present enzymatic activity of Crystal Structure of the Engineered Ssopox Variant IVA4:
3.1.8.1;

Protein crystallography data

The structure of Crystal Structure of the Engineered Ssopox Variant IVA4, PDB code: 8sfb was solved by P.Jacquet, R.Billot, A.Shimon, N.Hoekstra, C.Bergonzi, A.Jenks, D.Daude, M.H.Elias, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 68.78 / 1.40
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 64.47, 74.88, 137.55, 90, 90, 90
R / Rfree (%) 19.9 / 22.3

Other elements in 8sfb:

The structure of Crystal Structure of the Engineered Ssopox Variant IVA4 also contains other interesting chemical elements:

Iron (Fe) 1 atom

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Crystal Structure of the Engineered Ssopox Variant IVA4 (pdb code 8sfb). 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 the Engineered Ssopox Variant IVA4, PDB code: 8sfb:

Cobalt binding site 1 out of 1 in 8sfb

Go back to Cobalt Binding Sites List in 8sfb
Cobalt binding site 1 out of 1 in the Crystal Structure of the Engineered Ssopox Variant IVA4


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 the Engineered Ssopox Variant IVA4 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Co402

b:21.2
occ:0.75
O4 D:PO4403 1.8 50.7 0.8
O2 D:PO4403 1.9 70.3 0.8
ND1 D:HIS170 2.1 22.4 1.0
OQ2 D:KCX137 2.1 20.1 1.0
NE2 D:HIS199 2.1 22.2 1.0
P D:PO4403 2.2 103.7 0.8
CE1 D:HIS170 3.0 20.5 1.0
CE1 D:HIS199 3.0 23.1 1.0
CX D:KCX137 3.1 19.4 1.0
CG D:HIS170 3.1 19.8 1.0
CD2 D:HIS199 3.1 21.7 1.0
O1 D:PO4403 3.3 70.5 0.8
OQ1 D:KCX137 3.4 21.9 1.0
CB D:HIS170 3.5 18.6 1.0
O3 D:PO4403 3.5 64.1 0.8
NH2 D:ARG223 3.5 36.9 1.0
FE D:FE401 3.6 19.4 0.8
OD2 D:ASP256 4.1 33.0 1.0
NE2 D:HIS170 4.1 22.2 1.0
ND1 D:HIS199 4.2 22.4 1.0
CD2 D:HIS170 4.2 20.4 1.0
CA D:HIS170 4.2 16.3 1.0
CG D:HIS199 4.2 21.0 1.0
NZ D:KCX137 4.3 19.9 1.0
CZ D:ARG223 4.3 37.9 1.0
CE1 D:HIS22 4.4 21.6 1.0
NE2 D:HIS22 4.4 22.5 1.0
NE D:ARG223 4.7 32.5 1.0
CE D:KCX137 4.8 19.7 1.0
OD1 D:ASP256 4.9 27.1 1.0
CG D:ASP256 4.9 31.0 1.0

Reference:

P.Jacquet, R.Billot, A.Shimon, N.Hoekstra, C.Bergonzi, A.Jenks, E.Chabriere, D.Daude, M.H.Elias. Changes in Active Site Loops Conformation Relates to A Transition From Lactonase to Phosphotriesterase To Be Published.
Page generated: Tue Jul 30 20:01:51 2024

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