Iron in PDB 6rx4: The Structure of Bd Oxidase From Escherichia Coli

All present enzymatic activity of The Structure of Bd Oxidase From Escherichia Coli:
7.1.1.7;

The binding sites of Iron atom in the The Structure of Bd Oxidase From Escherichia Coli (pdb code 6rx4). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 3 binding sites of Iron where determined in the The Structure of Bd Oxidase From Escherichia Coli, PDB code: 6rx4:
Jump to Iron binding site number: 1; 2; 3;

Iron binding site 1 out of 3 in the The Structure of Bd Oxidase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Structure of Bd Oxidase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe601 b:52.3 occ:1.00 FE A:HEB601 0.0 52.3 1.0 NB A:HEB601 2.0 52.3 1.0 NA A:HEB601 2.1 52.3 1.0 NC A:HEB601 2.1 52.3 1.0 ND A:HEB601 2.1 52.3 1.0 NE2 A:HIS186 2.7 50.8 1.0 C4B A:HEB601 3.0 52.3 1.0 C1B A:HEB601 3.0 52.3 1.0 C1C A:HEB601 3.0 52.3 1.0 SD A:MET393 3.0 51.9 1.0 C1A A:HEB601 3.0 52.3 1.0 C4A A:HEB601 3.0 52.3 1.0 C4D A:HEB601 3.1 52.3 1.0 C1D A:HEB601 3.1 52.3 1.0 C4C A:HEB601 3.1 52.3 1.0 CHC A:HEB601 3.4 52.3 1.0 CE A:MET393 3.4 51.9 1.0 CHB A:HEB601 3.4 52.3 1.0 CHA A:HEB601 3.4 52.3 1.0 CD2 A:HIS186 3.5 50.8 1.0 CHD A:HEB601 3.5 52.3 1.0 CE1 A:HIS186 3.7 50.8 1.0 CG A:MET393 4.2 51.9 1.0 C3B A:HEB601 4.2 52.3 1.0 C2B A:HEB601 4.2 52.3 1.0 C2A A:HEB601 4.3 52.3 1.0 C2C A:HEB601 4.3 52.3 1.0 C3A A:HEB601 4.3 52.3 1.0 C3C A:HEB601 4.3 52.3 1.0 C3D A:HEB601 4.3 52.3 1.0 C2D A:HEB601 4.3 52.3 1.0 CG A:HIS186 4.7 50.8 1.0 ND1 A:HIS186 4.7 50.8 1.0

Iron binding site 2 out of 3 in the The Structure of Bd Oxidase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The Structure of Bd Oxidase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe602 b:54.9 occ:1.00 FE A:HEB602 0.0 54.9 1.0 NB A:HEB602 2.0 54.9 1.0 NA A:HEB602 2.1 54.9 1.0 NC A:HEB602 2.1 54.9 1.0 ND A:HEB602 2.1 54.9 1.0 C4B A:HEB602 2.9 54.9 1.0 C1C A:HEB602 3.0 54.9 1.0 C1B A:HEB602 3.0 54.9 1.0 C4A A:HEB602 3.0 54.9 1.0 C4D A:HEB602 3.0 54.9 1.0 C1A A:HEB602 3.1 54.9 1.0 C1D A:HEB602 3.1 54.9 1.0 C4C A:HEB602 3.1 54.9 1.0 CG A:GLU445 3.3 55.5 1.0 CHC A:HEB602 3.3 54.9 1.0 CHA A:HEB602 3.4 54.9 1.0 CHB A:HEB602 3.4 54.9 1.0 CD A:GLU445 3.5 55.5 1.0 CHD A:HEB602 3.6 54.9 1.0 OE2 A:GLU445 3.6 55.5 1.0 CE2 A:PHE12 3.6 55.3 1.0 CD2 A:PHE12 4.1 55.3 1.0 C3B A:HEB602 4.2 54.9 1.0 OE1 A:GLU445 4.2 55.5 1.0 C2B A:HEB602 4.2 54.9 1.0 C2C A:HEB602 4.2 54.9 1.0 C3A A:HEB602 4.3 54.9 1.0 C2A A:HEB602 4.3 54.9 1.0 C3D A:HEB602 4.3 54.9 1.0 C2D A:HEB602 4.3 54.9 1.0 C3C A:HEB602 4.3 54.9 1.0 CB A:GLU445 4.5 55.5 1.0 CZ A:PHE12 4.7 55.3 1.0 CB A:ALA16 4.8 53.8 1.0

Iron binding site 3 out of 3 in the The Structure of Bd Oxidase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of The Structure of Bd Oxidase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe603 b:52.4 occ:1.00 FE A:HDD603 0.0 52.4 1.0 ND A:HDD603 1.9 52.4 1.0 NB A:HDD603 1.9 52.4 1.0 NA A:HDD603 1.9 52.4 1.0 NC A:HDD603 1.9 52.4 1.0 NE2 A:HIS19 2.8 50.3 1.0 C4D A:HDD603 2.9 52.4 1.0 C1A A:HDD603 2.9 52.4 1.0 C1C A:HDD603 2.9 52.4 1.0 C4B A:HDD603 2.9 52.4 1.0 C4C A:HDD603 2.9 52.4 1.0 C4A A:HDD603 2.9 52.4 1.0 C1D A:HDD603 2.9 52.4 1.0 C1B A:HDD603 2.9 52.4 1.0 CHC A:HDD603 3.3 52.4 1.0 CHA A:HDD603 3.3 52.4 1.0 CHB A:HDD603 3.3 52.4 1.0 CHD A:HDD603 3.4 52.4 1.0 CE1 A:HIS19 3.5 50.3 1.0 CD2 A:HIS19 3.8 50.3 1.0 C2A A:HDD603 4.1 52.4 1.0 C3A A:HDD603 4.1 52.4 1.0 C2C A:HDD603 4.1 52.4 1.0 C3C A:HDD603 4.1 52.4 1.0 C2B A:HDD603 4.1 52.4 1.0 C3B A:HDD603 4.1 52.4 1.0 C3D A:HDD603 4.2 52.4 1.0 C2D A:HDD603 4.2 52.4 1.0 OND A:HDD603 4.5 52.4 1.0 CZ A:PHE104 4.7 56.1 1.0 ND1 A:HIS19 4.7 50.3 1.0 CAD A:HDD603 4.7 52.4 1.0 CA A:GLY70 4.8 53.4 1.0 CG2 A:VAL23 4.8 49.4 1.0 CG A:HIS19 4.8 50.3 1.0 OE2 A:GLU99 5.0 56.6 1.0

A.Thesseling, T.Rasmussen, S.Burschel, D.Wohlwend, J.Kagi, R.Muller, B.Bottcher, T.Friedrich. Homologous Bd Oxidases Share the Same Architecture But Differ in Mechanism. Nat Commun V. 10 5138 2019.
ISSN: ESSN 2041-1723
PubMed: 31723136
DOI: 10.1038/S41467-019-13122-4