Iron in PDB 3vpo: Crystal Structure of Human Ribonucleotide Reductase Subunit M2 (HRRM2) Mutant

All present enzymatic activity of Crystal Structure of Human Ribonucleotide Reductase Subunit M2 (HRRM2) Mutant:
1.17.4.1;

The structure of Crystal Structure of Human Ribonucleotide Reductase Subunit M2 (HRRM2) Mutant, PDB code: 3vpo was solved by X.Chen, Z.Xu, H.Liu, L.Zhang, B.Chen, L.Zhu, C.Yang, W.Zhu, J.Shao, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	35.59 / 2.30
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	109.032, 109.032, 175.900, 90.00, 90.00, 90.00
R / Rfree (%)	20.6 / 24

The structure of Crystal Structure of Human Ribonucleotide Reductase Subunit M2 (HRRM2) Mutant also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Iron atom in the Crystal Structure of Human Ribonucleotide Reductase Subunit M2 (HRRM2) Mutant (pdb code 3vpo). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Human Ribonucleotide Reductase Subunit M2 (HRRM2) Mutant, PDB code: 3vpo:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Human Ribonucleotide Reductase Subunit M2 (HRRM2) Mutant


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 Human Ribonucleotide Reductase Subunit M2 (HRRM2) Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe402 b:48.0 occ:0.50 OE1 A:GLU232 1.8 38.1 1.0 OE1 A:GLU266 2.1 33.9 1.0 OE2 A:GLU169 2.2 39.5 1.0 OE2 A:GLU266 2.2 34.6 1.0 ND1 A:HIS269 2.3 31.3 1.0 CD A:GLU266 2.5 33.6 1.0 CD A:GLU232 3.1 36.9 1.0 CD A:GLU169 3.1 36.3 1.0 CE1 A:HIS269 3.2 32.2 1.0 CG A:HIS269 3.4 32.8 1.0 OE1 A:GLU169 3.4 39.8 1.0 NE2 A:GLN165 3.7 27.1 1.0 CB A:HIS269 3.7 32.5 1.0 OE2 A:GLU232 3.9 38.2 1.0 CG A:GLU266 3.9 31.9 1.0 CG A:GLU232 4.0 36.9 1.0 CA A:GLU266 4.3 32.3 1.0 NE2 A:HIS269 4.3 31.4 1.0 CD2 A:HIS269 4.4 30.5 1.0 CG1 A:VAL141 4.5 33.5 1.0 CG A:GLU169 4.5 31.5 1.0 CD A:GLN165 4.5 30.3 1.0 CB A:GLU232 4.5 36.1 1.0 CB A:GLU266 4.6 31.9 1.0 CG A:GLN165 4.6 28.2 1.0 ND1 A:HIS172 4.8 31.0 1.0 CE1 A:HIS172 4.8 31.8 1.0 N A:GLU266 4.9 31.7 1.0 O A:ASP265 5.0 30.4 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Human Ribonucleotide Reductase Subunit M2 (HRRM2) Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Human Ribonucleotide Reductase Subunit M2 (HRRM2) Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe402 b:44.3 occ:0.50 OE1 B:GLU232 1.7 38.3 1.0 OE2 B:GLU169 2.1 38.4 1.0 OE2 B:GLU266 2.2 34.7 1.0 OE1 B:GLU266 2.2 35.8 1.0 ND1 B:HIS269 2.3 28.2 1.0 CD B:GLU266 2.5 35.0 1.0 CD B:GLU232 3.0 37.3 1.0 CD B:GLU169 3.1 37.3 1.0 CE1 B:HIS269 3.2 28.9 1.0 OE1 B:GLU169 3.4 40.5 1.0 CG B:HIS269 3.4 30.8 1.0 NE2 B:GLN165 3.6 30.1 1.0 CG B:GLU232 3.7 37.3 1.0 CB B:HIS269 3.8 32.8 1.0 OE2 B:GLU232 3.9 38.4 1.0 CG B:GLU266 4.0 33.6 1.0 CA B:GLU266 4.3 33.2 1.0 NE2 B:HIS269 4.4 31.0 1.0 CG B:GLU169 4.4 31.8 1.0 CG1 B:VAL141 4.4 34.8 1.0 CD2 B:HIS269 4.5 29.8 1.0 CD B:GLN165 4.5 31.0 1.0 CB B:GLU232 4.5 36.8 1.0 CB B:GLU266 4.6 32.8 1.0 CG B:GLN165 4.6 27.9 1.0 CE1 B:HIS172 4.8 28.3 1.0 ND1 B:HIS172 4.8 29.4 1.0 N B:GLU266 4.9 32.6 1.0 CE2 B:PHE236 5.0 36.9 1.0

X.Chen, Z.Xu, H.Liu, L.Zhang, B.Chen, L.Zhu, C.Yang, W.Zhu, J.Shao. Essential Role of E106 in the Proton-Coupled Electron Transfer in Human To Be Published.