Iron in PDB 7qbp: Crystal Structure of R2-Like Ligand-Binding Oxidase From Saccharopolyspora Erythraea

The structure of Crystal Structure of R2-Like Ligand-Binding Oxidase From Saccharopolyspora Erythraea, PDB code: 7qbp was solved by V.Srinivas, R.Diamanti, H.Lebrette, M.Hogbom, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.05 / 1.38
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	103.173, 103.173, 61.574, 90, 90, 90
R / Rfree (%)	15.2 / 16.5

The structure of Crystal Structure of R2-Like Ligand-Binding Oxidase From Saccharopolyspora Erythraea also contains other interesting chemical elements:

Manganese

(Mn)

1 atom

The binding sites of Iron atom in the Crystal Structure of R2-Like Ligand-Binding Oxidase From Saccharopolyspora Erythraea (pdb code 7qbp). 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 R2-Like Ligand-Binding Oxidase From Saccharopolyspora Erythraea, PDB code: 7qbp:

Iron binding site 1 out of 1 in the Crystal Structure of R2-Like Ligand-Binding Oxidase From Saccharopolyspora Erythraea


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 R2-Like Ligand-Binding Oxidase From Saccharopolyspora Erythraea within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe402 b:18.1 occ:1.00 OE2 A:GLU172 2.0 17.2 1.0 O A:HOH544 2.0 20.1 1.0 OE2 A:GLU106 2.0 18.1 1.0 OE1 A:GLU207 2.1 20.6 1.0 O2 A:PLM403 2.2 23.5 1.0 ND1 A:HIS210 2.3 16.8 1.0 HG2 A:GLU172 2.9 19.9 1.0 CD A:GLU172 3.0 18.8 1.0 CD A:GLU106 3.1 15.2 1.0 CD A:GLU207 3.1 24.8 1.0 HE1 A:PHE102 3.1 19.0 1.0 CE1 A:HIS210 3.1 16.4 1.0 C1 A:PLM403 3.2 22.4 1.0 HE1 A:HIS210 3.2 19.6 1.0 CG A:HIS210 3.4 15.7 1.0 MN A:MN3401 3.4 17.2 1.0 OE1 A:GLU106 3.4 17.4 1.0 OE2 A:GLU207 3.5 27.5 1.0 CG A:GLU172 3.5 16.6 1.0 O1 A:PLM403 3.5 25.0 1.0 HB2 A:HIS210 3.6 18.9 1.0 HB3 A:HIS210 3.6 18.9 1.0 CB A:HIS210 3.8 15.7 1.0 HA A:GLU207 3.8 20.9 1.0 HE1 A:TYR167 3.9 20.0 1.0 CE1 A:PHE102 4.0 15.9 1.0 OE1 A:GLU172 4.1 18.5 1.0 HG3 A:GLU172 4.1 19.9 1.0 HE1 A:HIS109 4.1 19.7 1.0 NE2 A:HIS210 4.3 15.7 1.0 HB3 A:GLU172 4.3 19.0 1.0 CG A:GLU106 4.3 15.3 1.0 HG23 A:VAL76 4.4 18.2 1.0 CG A:GLU207 4.4 20.4 1.0 CD2 A:HIS210 4.4 16.1 1.0 HZ A:PHE102 4.5 19.5 1.0 HG2 A:GLU106 4.5 18.4 1.0 HG3 A:GLU106 4.5 18.4 1.0 CB A:GLU172 4.6 15.8 1.0 HG3 A:GLU207 4.6 24.4 1.0 C2 A:PLM403 4.6 25.4 1.0 CZ A:PHE102 4.6 16.2 1.0 CA A:GLU207 4.7 17.4 1.0 H22 A:PLM403 4.7 30.4 1.0 HB2 A:GLU207 4.7 23.9 1.0 HD1 A:PHE102 4.7 18.5 1.0 CE1 A:HIS109 4.8 16.4 1.0 CD1 A:PHE102 4.8 15.4 1.0 ND1 A:HIS109 4.8 15.8 1.0 CE1 A:TYR167 4.8 16.7 1.0 O A:HOH502 4.8 30.9 1.0 CB A:GLU207 4.8 19.9 1.0 H21 A:PLM403 4.9 30.4 1.0

R.Diamanti, V.Srinivas, A.I.Johansson, A.Nordstrom, J.J.Griese, H.Lebrette, M.Hogbom. Comparative Structural Analysis Provides New Insights Into the Function of R2-Like Ligand-Binding Oxidase. Febs Lett. V. 596 1600 2022.
ISSN: ISSN 0014-5793
PubMed: 35175627
DOI: 10.1002/1873-3468.14319