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Calcium in PDB 8bt4: Ribonucleotide Reductase Class Ie R2 From Mesoplasma Florum, Radical- Lost Ground State

Enzymatic activity of Ribonucleotide Reductase Class Ie R2 From Mesoplasma Florum, Radical- Lost Ground State

All present enzymatic activity of Ribonucleotide Reductase Class Ie R2 From Mesoplasma Florum, Radical- Lost Ground State:
1.17.4.1;

Protein crystallography data

The structure of Ribonucleotide Reductase Class Ie R2 From Mesoplasma Florum, Radical- Lost Ground State, PDB code: 8bt4 was solved by H.Lebrette, V.Srinivas, M.Hogbom, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 48.62 / 1.35
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 175.503, 53.369, 79.03, 90, 108.38, 90
R / Rfree (%) 14.3 / 16.4

Calcium Binding Sites:

The binding sites of Calcium atom in the Ribonucleotide Reductase Class Ie R2 From Mesoplasma Florum, Radical- Lost Ground State (pdb code 8bt4). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Ribonucleotide Reductase Class Ie R2 From Mesoplasma Florum, Radical- Lost Ground State, PDB code: 8bt4:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 8bt4

Go back to Calcium Binding Sites List in 8bt4
Calcium binding site 1 out of 2 in the Ribonucleotide Reductase Class Ie R2 From Mesoplasma Florum, Radical- Lost Ground State


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Ribonucleotide Reductase Class Ie R2 From Mesoplasma Florum, Radical- Lost Ground State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca401

b:19.2
occ:0.80
O2 A:GOL402 2.2 46.5 1.0
O A:GLY266 2.3 24.8 1.0
OD2 A:ASP270 2.3 23.4 1.0
O A:HOH520 2.4 37.1 1.0
O1 A:GOL402 2.4 44.5 1.0
OD1 A:ASP269 2.4 25.1 1.0
C2 A:GOL402 3.1 51.0 1.0
C1 A:GOL402 3.1 50.0 1.0
CG A:ASP269 3.4 25.5 1.0
C A:GLY266 3.5 20.5 1.0
CG A:ASP270 3.5 26.3 1.0
OD2 A:ASP269 3.6 30.1 1.0
OD1 A:ASP270 4.0 36.9 1.0
O A:HOH553 4.1 31.1 1.0
CA A:GLY266 4.3 20.3 1.0
O A:HOH775 4.3 51.4 1.0
C3 A:GOL402 4.4 54.6 1.0
N A:LEU267 4.4 18.1 1.0
CA A:LEU267 4.4 17.2 1.0
O A:HOH563 4.6 33.4 1.0
N A:ASP270 4.6 18.6 1.0
CB A:ASP270 4.7 22.4 1.0
C A:LEU267 4.8 17.2 1.0
CB A:ASP269 4.8 22.5 1.0
O A:HOH672 4.8 49.3 1.0
O3 A:GOL402 4.9 57.2 1.0
N A:ASP269 4.9 19.9 1.0

Calcium binding site 2 out of 2 in 8bt4

Go back to Calcium Binding Sites List in 8bt4
Calcium binding site 2 out of 2 in the Ribonucleotide Reductase Class Ie R2 From Mesoplasma Florum, Radical- Lost Ground State


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Ribonucleotide Reductase Class Ie R2 From Mesoplasma Florum, Radical- Lost Ground State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca401

b:30.5
occ:0.80
O B:GLY266 2.1 36.1 1.0
O2 B:GOL402 2.3 51.8 1.0
OD1 B:ASP269 2.4 43.6 1.0
OD2 B:ASP270 2.4 29.2 0.7
O1 B:GOL402 2.5 53.5 1.0
C2 B:GOL402 3.0 55.2 1.0
CG B:ASP269 3.2 45.3 1.0
C B:GLY266 3.3 28.7 1.0
OD2 B:ASP269 3.4 49.2 1.0
C1 B:GOL402 3.4 55.1 1.0
CG B:ASP270 3.6 34.8 0.7
OD1 B:ASP270 4.0 38.6 0.7
CA B:GLY266 4.0 27.3 1.0
N B:LEU267 4.2 26.1 1.0
O B:HOH574 4.4 36.7 1.0
CA B:LEU267 4.4 25.1 1.0
C3 B:GOL402 4.5 56.1 1.0
C B:LEU267 4.6 27.9 1.0
CB B:ASP269 4.7 39.6 1.0
N B:ASP270 4.7 34.0 0.7
N B:ASP270 4.7 35.0 0.3
N B:ASP269 4.7 33.2 1.0
O B:HOH502 4.8 32.1 1.0
CB B:ASP270 4.8 35.4 0.7
O3 B:GOL402 4.9 57.3 1.0
N B:ALA268 4.9 29.0 1.0
OD1 B:ASP270 4.9 37.0 0.3

Reference:

H.Lebrette, V.Srinivas, J.John, O.Aurelius, R.Kumar, D.Lundin, A.S.Brewster, A.Bhowmick, A.Sirohiwal, I.S.Kim, S.Gul, C.Pham, K.D.Sutherlin, P.Simon, A.Butryn, P.Aller, A.M.Orville, F.D.Fuller, R.Alonso-Mori, A.Batyuk, N.K.Sauter, V.K.Yachandra, J.Yano, V.R.I.Kaila, B.M.Sjoberg, J.Kern, K.Roos, M.Hogbom. Structure of A Ribonucleotide Reductase R2 Protein Radical. Science V. 382 109 2023.
ISSN: ESSN 1095-9203
PubMed: 37797025
DOI: 10.1126/SCIENCE.ADH8160
Page generated: Thu Dec 28 01:35:45 2023

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