Atomistry » Iron » PDB 6f0b-6fl2 » 6f65
Atomistry »
  Iron »
    PDB 6f0b-6fl2 »
      6f65 »

Iron in PDB 6f65: R2-Like Ligand-Binding Oxidase A171F Mutant with Aerobically Reconstituted Mn/Fe Cofactor

Enzymatic activity of R2-Like Ligand-Binding Oxidase A171F Mutant with Aerobically Reconstituted Mn/Fe Cofactor

All present enzymatic activity of R2-Like Ligand-Binding Oxidase A171F Mutant with Aerobically Reconstituted Mn/Fe Cofactor:
1.17.4.1;

Protein crystallography data

The structure of R2-Like Ligand-Binding Oxidase A171F Mutant with Aerobically Reconstituted Mn/Fe Cofactor, PDB code: 6f65 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) 48.50 / 1.95
Space group I 2 2 2
Cell size a, b, c (Å), α, β, γ (°) 55.966, 97.196, 128.233, 90.00, 90.00, 90.00
R / Rfree (%) 17.7 / 20.7

Other elements in 6f65:

The structure of R2-Like Ligand-Binding Oxidase A171F Mutant with Aerobically Reconstituted Mn/Fe Cofactor also contains other interesting chemical elements:

Manganese (Mn) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the R2-Like Ligand-Binding Oxidase A171F Mutant with Aerobically Reconstituted Mn/Fe Cofactor (pdb code 6f65). 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 R2-Like Ligand-Binding Oxidase A171F Mutant with Aerobically Reconstituted Mn/Fe Cofactor, PDB code: 6f65:

Iron binding site 1 out of 1 in 6f65

Go back to Iron Binding Sites List in 6f65
Iron binding site 1 out of 1 in the R2-Like Ligand-Binding Oxidase A171F Mutant with Aerobically 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 A171F Mutant with Aerobically Reconstituted Mn/Fe Cofactor within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe401

b:39.4
occ:1.00
 OE2 A:GLU167 1.9 37.0 1.0
OE1 A:GLU102 2.1 41.6 1.0
OE2 A:GLU202 2.1 42.4 0.5
OE1 A:GLU202 2.2 36.6 0.5
ND1 A:HIS205 2.2 37.1 1.0
OE2 A:GLU202 2.4 41.5 0.5
O A:HOH525 2.4 48.5 1.0
CD A:GLU202 2.4 39.9 0.5
CD A:GLU167 3.0 40.9 1.0
HG2 A:GLU167 3.0 48.4 1.0
CE1 A:HIS205 3.1 35.7 1.0
CD A:GLU102 3.1 35.5 1.0
HE1 A:HIS205 3.1 42.9 1.0
CD A:GLU202 3.3 44.4 0.5
CG A:HIS205 3.3 33.1 1.0
OE2 A:GLU102 3.4 35.9 1.0
MN A:MN3402 3.5 36.7 1.0
HB2 A:HIS205 3.5 37.0 1.0
CG A:GLU167 3.5 40.3 1.0
OE1 A:GLU202 3.6 38.6 0.5
HB3 A:HIS205 3.6 37.0 1.0
CB A:HIS205 3.7 30.9 1.0
HE2 A:TYR162 3.7 53.8 1.0
HA A:GLU202 3.8 45.2 0.5
HA A:GLU202 3.8 45.3 0.5
CG A:GLU202 3.9 46.0 0.5
HE2 A:PHE98 3.9 45.5 1.0
OE1 A:GLU167 4.0 43.9 1.0
HE1 A:HIS105 4.0 38.1 1.0
HG21 A:VAL72 4.1 48.8 1.0
HG3 A:GLU167 4.2 48.4 1.0
CE2 A:PHE98 4.2 38.0 1.0
HZ A:PHE98 4.2 45.1 1.0
NE2 A:HIS205 4.2 37.1 1.0
HB3 A:GLU167 4.3 40.3 1.0
O A:HOH501 4.3 51.4 1.0
HD2 A:PHE171 4.3 61.5 1.0
HG2 A:GLU202 4.3 55.2 0.5
HG3 A:GLU202 4.3 55.2 0.5
CD2 A:HIS205 4.4 35.7 1.0
CZ A:PHE98 4.4 37.6 1.0
CG A:GLU102 4.5 33.2 1.0
HB3 A:GLU202 4.5 50.9 0.5
CB A:GLU167 4.5 33.6 1.0
CG A:GLU202 4.6 42.8 0.5
CB A:GLU202 4.6 42.5 0.5
HG2 A:GLU102 4.6 39.9 1.0
CA A:GLU202 4.6 37.8 0.5
CE2 A:TYR162 4.6 44.9 1.0
CE1 A:HIS105 4.6 31.8 1.0
HE2 A:PHE171 4.7 55.4 1.0
HG3 A:GLU102 4.7 39.9 1.0
CA A:GLU202 4.7 37.7 0.5
HG3 A:GLU202 4.7 51.4 0.5
ND1 A:HIS105 4.8 34.6 1.0
HB2 A:GLU202 4.9 51.6 0.5
CB A:GLU202 5.0 43.0 0.5
CD2 A:PHE98 5.0 36.4 1.0
HE2 A:HIS205 5.0 44.5 1.0
CG2 A:VAL72 5.0 40.7 1.0
HG11 A:VAL72 5.0 50.9 1.0

Reference:

J.J.Griese, R.Kositzki, M.Haumann, M.Hogbom. Assembly of A Heterodinuclear Mn/Fe Cofactor Is Coupled to Tyrosine-Valine Ether Cross-Link Formation in the R2-Like Ligand-Binding Oxidase. J. Biol. Inorg. Chem. V. 24 211 2019.
ISSN: ESSN 1432-1327
PubMed: 30689052
DOI: 10.1007/S00775-019-01639-4
Page generated: Tue Aug 6 18:00:58 2024

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy