Iron in PDB 6i95: R2-Like Ligand-Binding Oxidase G68L Mutant with Anaerobically Reconstituted Mn/Fe Cofactor

All present enzymatic activity of R2-Like Ligand-Binding Oxidase G68L Mutant with Anaerobically Reconstituted Mn/Fe Cofactor:
1.17.4.1;

The structure of R2-Like Ligand-Binding Oxidase G68L Mutant with Anaerobically Reconstituted Mn/Fe Cofactor, PDB code: 6i95 was solved by J.J.Griese, M.Hogbom, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.80 / 1.65
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	55.958, 97.602, 127.528, 90.00, 90.00, 90.00
R / Rfree (%)	17.3 / 20.4

The structure of R2-Like Ligand-Binding Oxidase G68L Mutant with Anaerobically Reconstituted Mn/Fe Cofactor also contains other interesting chemical elements:

Manganese

(Mn)

1 atom

The binding sites of Iron atom in the R2-Like Ligand-Binding Oxidase G68L Mutant with Anaerobically Reconstituted Mn/Fe Cofactor (pdb code 6i95). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the R2-Like Ligand-Binding Oxidase G68L Mutant with Anaerobically Reconstituted Mn/Fe Cofactor, PDB code: 6i95:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the R2-Like Ligand-Binding Oxidase G68L Mutant with Anaerobically Reconstituted Mn/Fe Cofactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of R2-Like Ligand-Binding Oxidase G68L Mutant with Anaerobically Reconstituted Mn/Fe Cofactor within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe402 b:27.9 occ:1.00 OE1 A:GLU167 2.0 33.0 1.0 OE2 A:GLU102 2.1 28.2 1.0 OE1 A:GLU202 2.1 27.1 1.0 ND1 A:HIS205 2.2 27.3 1.0 OE2 A:GLU167 2.2 28.7 1.0 OE2 A:GLU202 2.3 29.1 1.0 CD A:GLU167 2.4 27.4 1.0 CD A:GLU202 2.5 28.5 1.0 CE1 A:HIS205 3.0 25.8 1.0 CD A:GLU102 3.1 26.9 1.0 HE1 A:HIS205 3.2 31.0 1.0 CG A:HIS205 3.2 21.9 1.0 HB3 A:HIS205 3.4 33.3 1.0 OE1 A:GLU102 3.4 25.2 1.0 HB2 A:HIS205 3.5 33.3 1.0 HE2 A:PHE98 3.6 32.5 1.0 CB A:HIS205 3.6 27.7 1.0 MN A:MN401 3.7 26.9 1.0 CE2 A:PHE98 3.9 27.1 1.0 CG A:GLU167 3.9 30.8 1.0 HZ A:PHE98 4.0 33.4 1.0 CG A:GLU202 4.0 28.3 1.0 HA A:GLU202 4.0 33.1 1.0 HE2 A:TYR162 4.1 36.1 1.0 CZ A:PHE98 4.1 27.8 1.0 HB3 A:GLU167 4.2 36.7 1.0 NE2 A:HIS205 4.2 28.2 1.0 HG21 A:VAL72 4.2 33.5 1.0 HG2 A:GLU167 4.3 37.0 1.0 CD2 A:HIS205 4.3 26.1 1.0 HE1 A:HIS105 4.3 31.6 1.0 CG A:GLU102 4.3 25.0 1.0 HG2 A:GLU202 4.4 34.0 1.0 HG3 A:GLU167 4.4 37.0 1.0 O A:HOH551 4.4 40.4 1.0 O A:HOH511 4.4 36.1 1.0 HG2 A:GLU102 4.4 30.0 1.0 HG3 A:GLU202 4.4 34.0 1.0 HG3 A:GLU102 4.5 30.0 1.0 HB3 A:GLU202 4.6 35.2 1.0 CB A:GLU167 4.6 30.6 1.0 CD2 A:PHE98 4.6 27.3 1.0 O A:HOH502 4.7 43.5 1.0 CB A:GLU202 4.7 29.4 1.0 CA A:GLU202 4.8 27.6 1.0 HD2 A:PHE98 4.9 32.7 1.0 HB A:VAL72 4.9 28.8 1.0 CE2 A:TYR162 4.9 30.1 1.0 CE1 A:HIS105 4.9 26.4 1.0 CE1 A:PHE98 5.0 29.9 1.0 HE2 A:HIS205 5.0 33.9 1.0

Iron binding site 2 out of 2 in the R2-Like Ligand-Binding Oxidase G68L Mutant with Anaerobically Reconstituted Mn/Fe Cofactor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of R2-Like Ligand-Binding Oxidase G68L Mutant with Anaerobically Reconstituted Mn/Fe Cofactor within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe403 b:62.4 occ:0.99 O A:HOH557 2.1 58.9 1.0 O A:HOH558 2.2 56.6 1.0 NE2 A:HIS130 2.2 43.2 1.0 CD2 A:HIS130 3.2 49.4 1.0 CE1 A:HIS130 3.2 53.9 1.0 HD2 A:HIS130 3.3 59.3 1.0 HE1 A:HIS130 3.4 64.7 1.0 O A:HOH518 4.0 48.0 1.0 OD2 A:ASP129 4.2 61.8 1.0 CG A:HIS130 4.3 40.4 1.0 ND1 A:HIS130 4.3 44.8 1.0 OD1 A:ASP129 4.5 51.7 1.0 O A:HOH579 4.7 49.4 1.0 CG A:ASP129 4.8 58.1 1.0 HA3 A:GLY240 4.8 46.9 1.0

Y.Kutin, R.Kositzki, R.M.M.Branca, V.Srinivas, D.Lundin, M.Haumann, M.Hogbom, N.Cox, J.J.Griese. Chemical Flexibility of Heterobimetallic Mn/Fe Cofactors: R2LOX and R2C Proteins. J.Biol.Chem. 2019.
ISSN: ESSN 1083-351X
PubMed: 31591267
DOI: 10.1074/JBC.RA119.010570