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Iron in PDB 6y2n: Crystal Structure of Ribonucleotide Reductase R2 Subunit Solved By Serial Synchrotron Crystallography

Enzymatic activity of Crystal Structure of Ribonucleotide Reductase R2 Subunit Solved By Serial Synchrotron Crystallography

All present enzymatic activity of Crystal Structure of Ribonucleotide Reductase R2 Subunit Solved By Serial Synchrotron Crystallography:
1.17.4.1;

Protein crystallography data

The structure of Crystal Structure of Ribonucleotide Reductase R2 Subunit Solved By Serial Synchrotron Crystallography, PDB code: 6y2n was solved by A.Shilova, H.Lebrette, O.Aurelius, M.Hogbom, U.Mueller, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 59.30 / 2.40
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 64.320, 64.320, 153.150, 90.00, 90.00, 90.00
R / Rfree (%) 17.3 / 22.1

Other elements in 6y2n:

The structure of Crystal Structure of Ribonucleotide Reductase R2 Subunit Solved By Serial Synchrotron Crystallography also contains other interesting chemical elements:

Manganese (Mn) 1 atom

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Ribonucleotide Reductase R2 Subunit Solved By Serial Synchrotron Crystallography (pdb code 6y2n). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the Crystal Structure of Ribonucleotide Reductase R2 Subunit Solved By Serial Synchrotron Crystallography, PDB code: 6y2n:

Iron binding site 1 out of 1 in 6y2n

Go back to Iron Binding Sites List in 6y2n
Iron binding site 1 out of 1 in the Crystal Structure of Ribonucleotide Reductase R2 Subunit Solved By Serial Synchrotron Crystallography


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Ribonucleotide Reductase R2 Subunit Solved By Serial Synchrotron Crystallography within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe402

b:72.2
occ:0.76
 OE1 A:GLU205 1.7 97.3 1.0
O A:HOH517 2.1 77.3 0.8
OE2 A:GLU239 2.1 0.5 1.0
ND1 A:HIS242 2.2 81.9 1.0
O A:HOH502 2.3 87.5 0.8
OE1 A:GLU132 2.3 77.3 1.0
CD A:GLU205 2.9 84.9 1.0
MN A:MN3401 3.0 82.3 0.8
CD A:GLU239 3.0 0.1 1.0
CE1 A:HIS242 3.1 75.3 1.0
OE1 A:GLU239 3.2 0.8 1.0
CG A:HIS242 3.3 77.8 1.0
CD A:GLU132 3.3 79.0 1.0
CG A:GLU205 3.5 80.0 1.0
CB A:HIS242 3.6 66.9 1.0
OE2 A:GLU132 3.6 83.3 1.0
OE2 A:GLU205 3.9 98.8 1.0
NE2 A:GLN128 4.2 68.6 1.0
NE2 A:HIS242 4.2 85.5 1.0
CB A:GLU205 4.3 66.3 1.0
CD2 A:HIS242 4.3 75.3 1.0
CG A:GLU239 4.4 92.3 1.0
CG1 A:VAL104 4.4 70.8 1.0
CG A:GLU132 4.6 75.8 1.0
CE1 A:HIS135 4.7 71.3 1.0
CA A:GLU239 4.7 76.2 1.0
ND1 A:HIS135 4.7 68.7 1.0
CE2 A:PHE209 4.7 82.1 1.0
OE2 A:GLU101 4.8 0.7 1.0
CD2 A:PHE209 4.9 87.1 1.0
CG A:GLN128 4.9 68.9 1.0

Reference:

A.Shilova, H.Lebrette, O.Aurelius, J.Nan, M.Welin, R.Kovacic, S.Ghosh, C.Safari, R.J.Friel, M.Milas, Z.Matej, M.Hogbom, G.Branden, M.Kloos, R.L.Shoeman, B.Doak, T.Ursby, M.Hakansson, D.T.Logan, U.Mueller. Current Status and Future Opportunities For Serial Crystallography at Max IV Laboratory. J.Synchrotron Radiat. V. 27 1095 2020.
ISSN: ESSN 1600-5775
PubMed: 32876583
DOI: 10.1107/S1600577520008735
Page generated: Wed Aug 7 15:50:35 2024

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