Iron in PDB 7bet: Structure of Ribonucleotide Reductase R2 From Escherichia Coli Collected By Femtosecond Serial Crystallography on A Coc Membrane

All present enzymatic activity of Structure of Ribonucleotide Reductase R2 From Escherichia Coli Collected By Femtosecond Serial Crystallography on A Coc Membrane:
1.17.4.1;

The structure of Structure of Ribonucleotide Reductase R2 From Escherichia Coli Collected By Femtosecond Serial Crystallography on A Coc Membrane, PDB code: 7bet was solved by O.Aurelius, J.John, I.Martiel, M.Marsh, L.Vera, C.Y.Huang, V.Olieric, P.Leonarski, K.Nass, C.Padeste, A.Karpik, M.Hogbom, M.Wang, B.Pedrini, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.91 / 2.30
Space group	P 61 2 2
Cell size a, b, c (Å), α, β, γ (°)	91.6, 91.6, 207.2, 90, 90, 120
R / Rfree (%)	20.5 / 24.5

The binding sites of Iron atom in the Structure of Ribonucleotide Reductase R2 From Escherichia Coli Collected By Femtosecond Serial Crystallography on A Coc Membrane (pdb code 7bet). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of Ribonucleotide Reductase R2 From Escherichia Coli Collected By Femtosecond Serial Crystallography on A Coc Membrane, PDB code: 7bet:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of Ribonucleotide Reductase R2 From Escherichia Coli Collected By Femtosecond Serial Crystallography on A Coc Membrane


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Ribonucleotide Reductase R2 From Escherichia Coli Collected By Femtosecond Serial Crystallography on A Coc Membrane within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:60.8 occ:1.00 O A:HOH519 1.9 49.1 1.0 O A:HOH523 1.9 43.1 1.0 OE2 A:GLU204 1.9 63.7 1.0 OE2 A:GLU238 2.0 67.3 1.0 ND1 A:HIS241 2.1 51.3 1.0 OE1 A:GLU115 2.5 75.0 1.0 OE2 A:GLU115 3.0 52.4 1.0 CD A:GLU238 3.0 58.5 1.0 CD A:GLU204 3.0 66.8 1.0 CD A:GLU115 3.0 50.6 1.0 CE1 A:HIS241 3.0 60.9 1.0 CG A:HIS241 3.2 64.3 1.0 OE1 A:GLU238 3.3 57.9 1.0 FE A:FE402 3.3 59.8 1.0 CB A:HIS241 3.5 60.5 1.0 CG A:GLU204 3.7 58.7 1.0 NE1 A:TRP111 4.0 66.1 1.0 OE1 A:GLU204 4.0 63.5 1.0 NE2 A:HIS241 4.2 52.2 1.0 OD1 A:ASP84 4.2 55.7 1.0 CD2 A:HIS241 4.3 64.1 1.0 CG A:GLU238 4.3 55.0 1.0 O A:HOH507 4.4 60.5 1.0 CG A:GLU115 4.5 70.0 1.0 CA A:GLU238 4.5 58.1 1.0 CB A:GLU204 4.5 66.4 1.0 CD1 A:TRP111 4.5 56.6 1.0 CE1 A:HIS118 4.7 65.0 1.0 OE1 A:GLN87 4.7 62.0 1.0 ND1 A:HIS118 4.7 50.0 1.0 CB A:GLU238 4.8 58.6 1.0

Iron binding site 2 out of 2 in the Structure of Ribonucleotide Reductase R2 From Escherichia Coli Collected By Femtosecond Serial Crystallography on A Coc Membrane


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Ribonucleotide Reductase R2 From Escherichia Coli Collected By Femtosecond Serial Crystallography on A Coc Membrane within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe402 b:59.8 occ:1.00 O A:HOH519 2.1 49.1 1.0 ND1 A:HIS118 2.1 50.0 1.0 O A:HOH507 2.1 60.5 1.0 OE2 A:GLU115 2.2 52.4 1.0 OD2 A:ASP84 2.2 56.1 1.0 OD1 A:ASP84 2.5 55.7 1.0 CG A:ASP84 2.6 57.5 1.0 O A:HOH523 2.8 43.1 1.0 CE1 A:HIS118 2.9 65.0 1.0 CG A:HIS118 3.2 52.4 1.0 FE A:FE401 3.3 60.8 1.0 CD A:GLU115 3.4 50.6 1.0 CB A:HIS118 3.6 57.1 1.0 OE1 A:GLU238 3.7 57.9 1.0 OE1 A:GLU115 4.0 75.0 1.0 CB A:ASP84 4.1 62.0 1.0 NE2 A:HIS118 4.1 55.6 1.0 CD2 A:HIS118 4.2 55.9 1.0 CZ A:PHE208 4.3 54.2 1.0 CD A:GLU238 4.3 58.5 1.0 OE2 A:GLU238 4.3 67.3 1.0 CE1 A:HIS241 4.4 60.9 1.0 ND1 A:HIS241 4.5 51.3 1.0 CG2 A:ILE234 4.5 47.1 1.0 CE2 A:PHE208 4.5 63.5 1.0 CA A:GLU115 4.6 54.4 1.0 CG A:GLU115 4.6 70.0 1.0 CB A:GLU115 4.7 56.1 1.0 CE1 A:PHE208 4.8 59.8 1.0

I.Martiel, C.Pradervand, E.Panepucci, T.Zamofing, K.Nass, M.Marsh, L.Vera, C.Y.Hunag, V.Olieric, D.Buntschu, R.Kaelin, P.Leonarski, D.Ozerov, C.Padeste, A.Karpik, V.Thominet, J.Hora, N.Olieric, T.Weinert, M.Wranik, S.Brunle, J.Standfuss, O.Aurelius, J.John, M.Hogbom, L.Zhang, O.Einsle, G.Papp, S.Basu, F.Cipriani, P.Beaud, R.Mankowsky, W.Glettig, A.Mozzanica, S.Redford, B.Schmidt, O.Bunk, R.Abela, M.Wang, H.Lemke, B.Pedrini. Commissioning Results From the Swissmx Instrument For Fixed Target Macromolecular Crystallography at Swissfel To Be Published.