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Cobalt in PDB 1h0n: Cobalt Substitution of Mouse R2 Ribonucleotide Reductase to Model the Reactive Diferrous State

Enzymatic activity of Cobalt Substitution of Mouse R2 Ribonucleotide Reductase to Model the Reactive Diferrous State

All present enzymatic activity of Cobalt Substitution of Mouse R2 Ribonucleotide Reductase to Model the Reactive Diferrous State:
1.17.4.1;

Protein crystallography data

The structure of Cobalt Substitution of Mouse R2 Ribonucleotide Reductase to Model the Reactive Diferrous State, PDB code: 1h0n was solved by K.R.Strand, S.Karlsen, K.K.Andersson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 8.0 / 2.4
Space group C 2 2 21
Cell size a, b, c (Å), α, β, γ (°) 75.100, 106.860, 91.460, 90.00, 90.00, 90.00
R / Rfree (%) 21.8 / 29.7

Cobalt Binding Sites:

The binding sites of Cobalt atom in the Cobalt Substitution of Mouse R2 Ribonucleotide Reductase to Model the Reactive Diferrous State (pdb code 1h0n). This binding sites where shown within 5.0 Angstroms radius around Cobalt atom.
In total 2 binding sites of Cobalt where determined in the Cobalt Substitution of Mouse R2 Ribonucleotide Reductase to Model the Reactive Diferrous State, PDB code: 1h0n:
Jump to Cobalt binding site number: 1; 2;

Cobalt binding site 1 out of 2 in 1h0n

Go back to Cobalt Binding Sites List in 1h0n
Cobalt binding site 1 out of 2 in the Cobalt Substitution of Mouse R2 Ribonucleotide Reductase to Model the Reactive Diferrous State


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 1 of Cobalt Substitution of Mouse R2 Ribonucleotide Reductase to Model the Reactive Diferrous State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co1353

b:38.6
occ:1.00
OD2 A:ASP139 1.8 29.7 1.0
ND1 A:HIS173 2.1 24.9 1.0
OE1 A:GLU170 2.2 33.1 1.0
CG A:ASP139 2.4 31.9 1.0
OD1 A:ASP139 2.5 31.2 1.0
OE2 A:GLU267 2.5 45.0 1.0
CD A:GLU267 2.8 40.7 1.0
OE1 A:GLU267 2.9 36.6 1.0
CE1 A:HIS173 3.0 25.0 1.0
CD A:GLU170 3.2 28.7 1.0
CG A:HIS173 3.2 24.0 1.0
CO A:CO1354 3.4 30.5 1.0
OE2 A:GLU170 3.5 29.5 1.0
CB A:HIS173 3.7 25.7 1.0
CG A:GLU267 3.9 41.1 1.0
CB A:ASP139 3.9 34.3 1.0
O A:HOH2081 4.0 45.4 1.0
NE2 A:HIS173 4.1 24.5 1.0
OE2 A:GLU233 4.2 34.8 1.0
CD2 A:HIS173 4.3 23.2 1.0
CG A:GLU170 4.5 27.2 1.0
CA A:GLU170 4.6 23.1 1.0
ND1 A:HIS270 4.6 18.6 1.0
CE1 A:HIS270 4.6 20.1 1.0
CG2 A:ILE263 4.6 36.3 1.0
CB A:GLU170 4.9 22.9 1.0
CA A:ASP139 5.0 35.6 1.0

Cobalt binding site 2 out of 2 in 1h0n

Go back to Cobalt Binding Sites List in 1h0n
Cobalt binding site 2 out of 2 in the Cobalt Substitution of Mouse R2 Ribonucleotide Reductase to Model the Reactive Diferrous State


Mono view


Stereo pair view

A full contact list of Cobalt with other atoms in the Co binding site number 2 of Cobalt Substitution of Mouse R2 Ribonucleotide Reductase to Model the Reactive Diferrous State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Co1354

b:30.5
occ:1.00
OE2 A:GLU233 1.7 34.8 1.0
OE1 A:GLU267 1.8 36.6 1.0
OE2 A:GLU170 2.0 29.5 1.0
CD A:GLU233 2.2 36.4 1.0
ND1 A:HIS270 2.2 18.6 1.0
OE1 A:GLU233 2.4 29.8 1.0
CD A:GLU267 2.8 40.7 1.0
CD A:GLU170 3.0 28.7 1.0
CE1 A:HIS270 3.1 20.1 1.0
OE2 A:GLU267 3.2 45.0 1.0
CG A:HIS270 3.3 22.7 1.0
OE1 A:GLU170 3.3 33.1 1.0
CO A:CO1353 3.4 38.6 1.0
CG A:GLU233 3.5 33.3 1.0
CB A:HIS270 3.6 24.3 1.0
NE2 A:GLN166 3.7 31.2 1.0
OD1 A:ASP139 4.1 31.2 1.0
CG A:GLU267 4.2 41.1 1.0
NE2 A:HIS270 4.3 21.1 1.0
CG A:GLU170 4.3 27.2 1.0
CB A:GLU233 4.4 33.2 1.0
CD2 A:HIS270 4.4 20.5 1.0
CA A:GLU267 4.4 36.2 1.0
CG1 A:VAL142 4.5 26.4 1.0
CB A:GLU267 4.6 36.9 1.0
CD A:GLN166 4.6 27.8 1.0
OD2 A:ASP139 4.7 29.7 1.0
CG A:GLN166 4.7 24.4 1.0
CG A:ASP139 4.7 31.9 1.0
ND1 A:HIS173 4.9 24.9 1.0
CG2 A:VAL142 4.9 32.5 1.0
N A:GLU267 5.0 36.1 1.0

Reference:

K.R.Strand, S.Karlsen, K.K.Andersson. Cobalt Substitution of Mouse R2 Ribonucleotide Reductase As A Model For Thereactive Diferrous State. Spectroscopic and Structural Evidence For A Ferromagnetically Coupled Dinuclear Cobalt Cluster J.Biol.Chem. V. 277 34229 2002.
ISSN: ISSN 0021-9258
PubMed: 12087093
DOI: 10.1074/JBC.M203358200
Page generated: Sun Dec 13 10:34:59 2020

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