Iron in PDB 5g5g: Escherichia Coli Periplasmic Aldehyde Oxidase

The structure of Escherichia Coli Periplasmic Aldehyde Oxidase, PDB code: 5g5g was solved by M.A.S.Correia, A.R.Otrelo-Cardoso, M.J.Romao, T.Santos-Silva, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.32 / 1.70
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	109.681, 78.342, 151.909, 90.00, 99.69, 90.00
R / Rfree (%)	13.8 / 16.7

The structure of Escherichia Coli Periplasmic Aldehyde Oxidase also contains other interesting chemical elements:

Molybdenum	(Mo)	1 atom
Iodine	(I)	7 atoms
Chlorine	(Cl)	12 atoms

The binding sites of Iron atom in the Escherichia Coli Periplasmic Aldehyde Oxidase (pdb code 5g5g). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the Escherichia Coli Periplasmic Aldehyde Oxidase, PDB code: 5g5g:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Iron binding site 1 out of 8 in the Escherichia Coli Periplasmic Aldehyde Oxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Escherichia Coli Periplasmic Aldehyde Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe230 b:10.6 occ:1.00 FE1 A:FES230 0.0 10.6 1.0 SG A:CYS161 2.2 11.2 1.0 SG A:CYS208 2.2 10.1 1.0 S2 A:FES230 2.2 11.1 1.0 S1 A:FES230 2.2 11.6 1.0 CB A:CYS208 3.1 10.2 1.0 FE2 A:FES230 3.1 10.3 1.0 CB A:CYS161 3.3 10.3 1.0 CA A:CYS208 3.4 10.0 1.0 O A:HOH2122 4.1 11.3 1.0 C A:CYS208 4.2 10.3 1.0 N A:CYS161 4.2 10.0 1.0 N A:ARG209 4.3 9.9 1.0 CA A:CYS161 4.3 10.6 1.0 CB A:CYS210 4.4 10.0 1.0 N A:CYS210 4.5 9.4 1.0 SG A:CYS210 4.5 10.0 1.0 O A:ILE207 4.6 10.9 1.0 N A:CYS208 4.6 10.6 1.0 C A:CYS161 4.9 10.0 1.0 SG A:CYS158 4.9 9.8 1.0 O A:CYS208 5.0 9.7 1.0 CA A:CYS210 5.0 9.6 1.0 NE2 A:GLN165 5.0 11.1 1.0

Iron binding site 2 out of 8 in the Escherichia Coli Periplasmic Aldehyde Oxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Escherichia Coli Periplasmic Aldehyde Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe230 b:10.3 occ:1.00 FE2 A:FES230 0.0 10.3 1.0 SG A:CYS158 2.2 9.8 1.0 SG A:CYS210 2.2 10.0 1.0 S1 A:FES230 2.2 11.6 1.0 S2 A:FES230 2.2 11.1 1.0 FE1 A:FES230 3.1 10.6 1.0 CB A:CYS158 3.1 10.1 1.0 CB A:CYS210 3.4 10.0 1.0 N A:CYS158 3.4 9.9 1.0 O A:HOH2126 3.6 10.2 1.0 CA A:CYS158 3.7 9.9 1.0 N A:GLY159 3.9 9.5 1.0 N A:CYS210 4.1 9.4 1.0 C A:CYS158 4.2 9.8 1.0 CA A:CYS210 4.3 9.6 1.0 N A:TYR160 4.3 9.5 1.0 SG A:CYS208 4.5 10.1 1.0 C A:GLN157 4.6 10.3 1.0 N A:GLN157 4.8 10.1 1.0 CB A:GLN157 4.8 10.9 1.0 N A:CYS161 4.8 10.0 1.0 SG A:CYS161 4.9 11.2 1.0 CA A:GLN157 5.0 10.5 1.0 CA A:GLY159 5.0 9.9 1.0

Iron binding site 3 out of 8 in the Escherichia Coli Periplasmic Aldehyde Oxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Escherichia Coli Periplasmic Aldehyde Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe231 b:10.6 occ:1.00 FE1 A:FES231 0.0 10.6 1.0 S2 A:FES231 2.2 9.8 1.0 S1 A:FES231 2.2 9.7 1.0 SG A:CYS107 2.3 12.3 1.0 SG A:CYS119 2.3 11.4 1.0 FE2 A:FES231 2.7 10.2 1.0 CB A:CYS119 3.3 11.5 1.0 CB A:CYS107 3.3 10.8 1.0 N A:CYS119 4.2 11.1 1.0 N A:GLY102 4.3 10.6 1.0 N A:CYS107 4.3 11.0 1.0 CA A:CYS119 4.3 11.7 1.0 SG A:CYS99 4.3 11.2 1.0 CB A:ASN117 4.3 12.5 1.0 CA A:CYS107 4.5 10.8 1.0 N A:ASP100 4.5 11.2 1.0 CA A:GLY102 4.5 10.4 1.0 SG A:CYS104 4.6 10.2 1.0 CG A:ASN117 4.6 13.0 1.0 CA A:ASP100 4.7 11.4 1.0 N A:GLY105 4.8 10.9 1.0 N A:HIS101 4.8 10.9 1.0 CD2 A:LEU83 4.8 11.0 1.0 N A:ALA106 4.9 10.5 1.0 C A:ASP100 5.0 11.1 1.0

Iron binding site 4 out of 8 in the Escherichia Coli Periplasmic Aldehyde Oxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Escherichia Coli Periplasmic Aldehyde Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe231 b:10.2 occ:1.00 FE2 A:FES231 0.0 10.2 1.0 S1 A:FES231 2.2 9.7 1.0 S2 A:FES231 2.3 9.8 1.0 SG A:CYS104 2.3 10.2 1.0 SG A:CYS99 2.4 11.2 1.0 FE1 A:FES231 2.7 10.6 1.0 CB A:CYS104 3.5 10.2 1.0 CB A:CYS99 3.5 11.2 1.0 N A:CYS99 3.5 11.1 1.0 N A:CYS104 3.6 11.3 1.0 N A:ASP100 3.9 11.2 1.0 CA A:CYS99 3.9 11.3 1.0 CA A:CYS104 3.9 10.6 1.0 N A:GLY105 3.9 10.9 1.0 N A:GLN103 4.1 10.7 1.0 C A:GLY98 4.2 11.2 1.0 N A:GLY98 4.3 10.7 1.0 C A:CYS104 4.3 10.5 1.0 C A:CYS99 4.3 11.8 1.0 N A:ALA106 4.3 10.5 1.0 CA A:GLY98 4.4 10.7 1.0 N A:GLY102 4.4 10.6 1.0 SG A:CYS119 4.4 11.4 1.0 SG A:CYS107 4.6 12.3 1.0 C A:GLN103 4.6 11.5 1.0 N A:HIS101 4.7 10.9 1.0 C A:GLY102 4.7 11.1 1.0 CA A:GLY102 4.8 10.4 1.0 CA A:GLN103 4.8 11.4 1.0 CA A:ASP100 4.9 11.4 1.0 CA A:GLY105 4.9 10.5 1.0

Iron binding site 5 out of 8 in the Escherichia Coli Periplasmic Aldehyde Oxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Escherichia Coli Periplasmic Aldehyde Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe320 b:16.9 occ:1.00 FE1 B:SF4320 0.0 16.9 1.0 SG B:CYS138 2.1 19.8 1.0 S4 B:SF4320 2.3 20.5 1.0 S2 B:SF4320 2.4 18.9 1.0 S3 B:SF4320 2.4 19.6 1.0 CB B:CYS138 3.0 21.5 1.0 FE4 B:SF4320 3.1 16.9 1.0 FE2 B:SF4320 3.2 17.9 1.0 CA B:CYS138 3.3 21.6 1.0 FE3 B:SF4320 3.3 16.0 1.0 C B:CYS138 3.9 21.6 1.0 S1 B:SF4320 4.0 17.6 1.0 N B:ALA139 4.0 21.1 1.0 N B:ALA140 4.2 20.0 1.0 O B:ALA156 4.3 22.3 1.0 CB B:ALA140 4.3 18.8 1.0 CA B:CYS157 4.3 20.3 1.0 N B:ILE158 4.6 18.5 1.0 SG B:CYS157 4.6 18.5 1.0 N B:CYS138 4.7 23.4 1.0 O B:CYS138 4.7 21.9 1.0 CB B:CYS157 4.8 20.0 1.0 CA B:ALA140 4.8 19.6 1.0 O B:GLY137 4.9 22.8 1.0 SG B:CYS129 4.9 18.8 1.0 CA B:CYS129 5.0 19.3 1.0 N B:ASN130 5.0 20.6 1.0

Iron binding site 6 out of 8 in the Escherichia Coli Periplasmic Aldehyde Oxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Escherichia Coli Periplasmic Aldehyde Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe320 b:17.9 occ:1.00 FE2 B:SF4320 0.0 17.9 1.0 SG B:CYS129 1.8 18.8 1.0 S4 B:SF4320 2.2 20.5 1.0 S3 B:SF4320 2.3 19.6 1.0 S1 B:SF4320 2.5 17.6 1.0 CB B:CYS129 2.9 18.7 1.0 FE1 B:SF4320 3.2 16.9 1.0 FE3 B:SF4320 3.2 16.0 1.0 CA B:CYS129 3.3 19.3 1.0 FE4 B:SF4320 3.4 16.9 1.0 C B:CYS129 3.7 20.3 1.0 N B:ASN130 3.8 20.6 1.0 N B:LYS131 3.9 21.2 1.0 CB B:LYS131 3.9 20.6 1.0 S2 B:SF4320 4.1 18.9 1.0 CB B:PHE122 4.4 16.6 1.0 CA B:PHE122 4.4 16.9 1.0 N B:PHE122 4.5 16.4 1.0 O B:CYS129 4.5 20.0 1.0 CA B:LYS131 4.6 21.8 1.0 N B:CYS129 4.6 20.3 1.0 SG B:CYS119 4.6 15.6 1.0 O B:PRO128 4.7 22.2 1.0 CA B:ASN130 4.9 21.6 1.0 C B:ASN130 4.9 21.9 1.0 N B:ARG132 4.9 24.3 1.0

Iron binding site 7 out of 8 in the Escherichia Coli Periplasmic Aldehyde Oxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Escherichia Coli Periplasmic Aldehyde Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe320 b:16.0 occ:1.00 FE3 B:SF4320 0.0 16.0 1.0 SG B:CYS119 2.0 15.6 1.0 S1 B:SF4320 2.2 17.6 1.0 S4 B:SF4320 2.3 20.5 1.0 S2 B:SF4320 2.4 18.9 1.0 CB B:CYS119 2.9 15.5 1.0 FE2 B:SF4320 3.2 17.9 1.0 FE4 B:SF4320 3.3 16.9 1.0 FE1 B:SF4320 3.3 16.9 1.0 NE2 B:HIS148 3.8 18.7 1.0 S3 B:SF4320 4.1 19.6 1.0 CD2 B:HIS148 4.2 18.8 1.0 CA B:CYS119 4.3 14.9 1.0 CB B:ALA140 4.3 18.8 1.0 N B:PHE122 4.4 16.4 1.0 CB B:PHE122 4.4 16.6 1.0 CB B:ALA159 4.5 16.4 1.0 SG B:CYS129 4.7 18.8 1.0 CB B:TYR121 4.8 17.3 1.0 C B:CYS119 4.9 15.0 1.0 CE1 B:HIS148 4.9 19.3 1.0 CA B:PHE122 4.9 16.9 1.0

Iron binding site 8 out of 8 in the Escherichia Coli Periplasmic Aldehyde Oxidase


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Escherichia Coli Periplasmic Aldehyde Oxidase within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe320 b:16.9 occ:1.00 FE4 B:SF4320 0.0 16.9 1.0 SG B:CYS157 1.9 18.5 1.0 S2 B:SF4320 2.2 18.9 1.0 S3 B:SF4320 2.3 19.6 1.0 S1 B:SF4320 2.4 17.6 1.0 CB B:CYS157 3.0 20.0 1.0 FE1 B:SF4320 3.1 16.9 1.0 FE3 B:SF4320 3.3 16.0 1.0 FE2 B:SF4320 3.4 17.9 1.0 CB B:ALA159 3.6 16.4 1.0 CA B:CYS157 3.6 20.3 1.0 N B:ALA159 3.9 17.1 1.0 N B:ILE158 4.0 18.5 1.0 S4 B:SF4320 4.0 20.5 1.0 C B:CYS157 4.1 19.7 1.0 CE B:LYS131 4.2 19.7 1.0 CA B:ALA159 4.3 16.6 1.0 CB B:LYS131 4.4 20.6 1.0 SG B:CYS138 4.7 19.8 1.0 O B:ALA156 4.7 22.3 1.0 C B:ILE158 4.8 17.7 1.0 CD B:LYS131 4.9 19.6 1.0 N B:CYS157 4.9 21.9 1.0 SG B:CYS129 4.9 18.8 1.0 CA B:ILE158 5.0 18.4 1.0 O B:HOH2141 5.0 38.6 1.0

M.A.Correia, A.R.Otrelo-Cardoso, V.Schwuchow, K.G.Sigfridsson Clauss, M.Haumann, M.J.Romao, S.Leimkuhler, T.Santos-Silva. The Escherichia Coli Periplasmic Aldehyde Oxidoreductase Is An Exceptional Member of the Xanthine Oxidase Family of Molybdoenzymes. Acs Chem.Biol. V. 11 2923 2016.
ISSN: ISSN 1554-8929
PubMed: 27622978
DOI: 10.1021/ACSCHEMBIO.6B00572