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Cobalt in PDB 3vyh: Crystal Structure of AW116R Mutant of Nitrile Hydratase From Pseudonocardia Thermophilla

Enzymatic activity of Crystal Structure of AW116R Mutant of Nitrile Hydratase From Pseudonocardia Thermophilla

All present enzymatic activity of Crystal Structure of AW116R Mutant of Nitrile Hydratase From Pseudonocardia Thermophilla:
4.2.1.84;

Protein crystallography data

The structure of Crystal Structure of AW116R Mutant of Nitrile Hydratase From Pseudonocardia Thermophilla, PDB code: 3vyh was solved by Y.Yamanaka, M.Sato, T.Arakawa, S.Namima, S.Hori, A.Ohtaki, K.Noguchi, Y.Katayama, M.Yohda, M.Odaka, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.44 / 1.63
Space group P 32 2 1
Cell size a, b, c (Å), α, β, γ (°) 65.683, 65.683, 184.796, 90.00, 90.00, 120.00
R / Rfree (%) 17.4 / 20.3

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Crystal Structure of AW116R Mutant of Nitrile Hydratase From Pseudonocardia Thermophilla (pdb code 3vyh). 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 AW116R Mutant of Nitrile Hydratase From Pseudonocardia Thermophilla, PDB code: 3vyh:

Cobalt binding site 1 out of 1 in 3vyh

Go back to Cobalt Binding Sites List in 3vyh
Cobalt binding site 1 out of 1 in the Crystal Structure of AW116R Mutant of Nitrile Hydratase From Pseudonocardia Thermophilla


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 AW116R Mutant of Nitrile Hydratase From Pseudonocardia Thermophilla within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co301

b:10.9
occ:1.00
 N A:CSO113 1.9 10.6 1.0
N A:SER112 2.0 10.4 1.0
SG A:CSD111 2.1 11.5 1.0
SG A:CSO113 2.2 13.1 1.0
O A:HOH527 2.3 29.2 1.0
SG A:CYS108 2.3 10.9 1.0
C A:SER112 2.7 11.6 1.0
CA A:SER112 2.8 10.8 1.0
CA A:CSO113 2.9 10.8 1.0
OD1 A:CSD111 3.0 13.8 1.0
CB A:CSO113 3.0 11.0 1.0
C A:CSD111 3.1 9.1 1.0
CB A:CSD111 3.1 9.1 1.0
OD A:CSO113 3.1 16.6 1.0
OD2 A:CSD111 3.2 12.6 1.0
CB A:CYS108 3.3 9.6 1.0
CA A:CSD111 3.4 9.5 1.0
OG A:SER112 3.8 18.9 1.0
N A:CSD111 3.8 9.7 1.0
O A:SER112 3.9 10.7 1.0
CB A:SER112 3.9 12.9 1.0
O A:CSD111 4.2 12.2 1.0
C A:CSO113 4.3 11.2 1.0
O A:CSO113 4.6 12.3 1.0
CA A:CYS108 4.7 8.3 1.0
NH2 B:ARG157 4.8 10.1 1.0
C A:LEU110 4.9 9.2 1.0
O A:CYS108 4.9 12.0 1.0

Reference:

Y.Yamanaka, M.Sato, T.Arakawa, S.Namima, S.Hori, A.Ohtaki, K.Noguchi, Y.Katayama, M.Yohda, M.Odaka. Effects of Argnine Residue Around the Substrate Pocket on the Substrate Specificity of Thiocyanate Hydrolase To Be Published.
Page generated: Tue Jul 30 16:48:48 2024

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