Iron in PDB 6tqh: Escherichia Coli Adhe Structure in Its Extended Conformation

All present enzymatic activity of Escherichia Coli Adhe Structure in Its Extended Conformation:
1.1.1.1; 1.2.1.10;

The binding sites of Iron atom in the Escherichia Coli Adhe Structure in Its Extended Conformation (pdb code 6tqh). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Escherichia Coli Adhe Structure in Its Extended Conformation, PDB code: 6tqh:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Escherichia Coli Adhe Structure in Its Extended Conformation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Escherichia Coli Adhe Structure in Its Extended Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe903 b:90.3 occ:1.00 HE1 A:HIS737 1.1 81.8 1.0 NE2 A:HIS657 1.7 76.2 1.0 OD2 A:ASP653 2.0 79.4 1.0 OD1 A:ASP653 2.0 79.4 1.0 CE1 A:HIS737 2.1 81.8 1.0 NE2 A:HIS723 2.1 77.6 1.0 H5N A:NAD901 2.1 86.4 1.0 CG A:ASP653 2.3 79.4 1.0 CD2 A:HIS657 2.7 76.2 1.0 CE1 A:HIS657 2.7 76.2 1.0 C5N A:NAD901 2.8 86.4 1.0 HD22 A:ASN741 2.9 80.3 1.0 HD2 A:HIS657 2.9 76.2 1.0 HE1 A:HIS657 3.0 76.2 1.0 CD2 A:HIS723 3.0 77.6 1.0 ND1 A:HIS737 3.0 81.8 1.0 NE2 A:HIS737 3.0 81.8 1.0 CE1 A:HIS723 3.1 77.6 1.0 HD2 A:HIS723 3.1 77.6 1.0 HD1 A:HIS737 3.2 81.8 1.0 HD21 A:ASN741 3.2 80.3 1.0 HE1 A:HIS723 3.3 77.6 1.0 ND2 A:ASN741 3.4 80.3 1.0 H6N A:NAD901 3.5 86.4 1.0 C6N A:NAD901 3.6 86.4 1.0 C4N A:NAD901 3.7 86.4 1.0 ND1 A:HIS657 3.7 76.2 1.0 CG A:HIS657 3.8 76.2 1.0 H4N A:NAD901 3.8 86.4 1.0 CB A:ASP653 3.8 79.4 1.0 HB3 A:ASP653 4.1 79.4 1.0 CG A:HIS723 4.2 77.6 1.0 O A:ASP653 4.2 79.4 1.0 ND1 A:HIS723 4.2 77.6 1.0 CD2 A:HIS737 4.2 81.8 1.0 CG A:HIS737 4.2 81.8 1.0 HB2 A:ASP653 4.3 79.4 1.0 HG1 A:THR656 4.5 77.4 1.0 HA A:ASP653 4.5 79.4 1.0 HD1 A:HIS657 4.5 76.2 1.0 CA A:ASP653 4.6 79.4 1.0 HD11 A:LEU719 4.6 77.0 1.0 C A:ASP653 4.6 79.4 1.0 CG A:ASN741 4.7 80.3 1.0 HA A:THR601 4.7 82.0 1.0 OG1 A:THR656 4.7 77.4 1.0 N1N A:NAD901 4.8 86.4 1.0 HG A:LEU719 4.8 77.0 1.0 C3N A:NAD901 4.9 86.4 1.0 HD1 A:HIS723 5.0 77.6 1.0 HE2 A:HIS727 5.0 82.2 1.0

Iron binding site 2 out of 2 in the Escherichia Coli Adhe Structure in Its Extended Conformation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Escherichia Coli Adhe Structure in Its Extended Conformation within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe903 b:85.7 occ:1.00 HE1 B:HIS737 1.1 79.0 1.0 NE2 B:HIS657 1.7 73.9 1.0 OD2 B:ASP653 2.0 76.8 1.0 OD1 B:ASP653 2.1 76.8 1.0 CE1 B:HIS737 2.1 79.0 1.0 NE2 B:HIS723 2.1 74.8 1.0 CG B:ASP653 2.3 76.8 1.0 CD2 B:HIS657 2.7 73.9 1.0 CE1 B:HIS657 2.7 73.9 1.0 HD22 B:ASN741 2.9 77.4 1.0 HD2 B:HIS657 2.9 73.9 1.0 H5N B:NAD902 2.9 83.8 1.0 CD2 B:HIS723 3.0 74.8 1.0 HE1 B:HIS657 3.0 73.9 1.0 NE2 B:HIS737 3.0 79.0 1.0 ND1 B:HIS737 3.0 79.0 1.0 CE1 B:HIS723 3.1 74.8 1.0 HD2 B:HIS723 3.1 74.8 1.0 HD1 B:HIS737 3.2 79.0 1.0 HD21 B:ASN741 3.2 77.4 1.0 HE1 B:HIS723 3.3 74.8 1.0 ND2 B:ASN741 3.4 77.4 1.0 C5N B:NAD902 3.4 83.8 1.0 H4N B:NAD902 3.5 83.8 1.0 C4N B:NAD902 3.7 83.8 1.0 ND1 B:HIS657 3.7 73.9 1.0 CG B:HIS657 3.8 73.9 1.0 CB B:ASP653 3.8 76.8 1.0 CG B:HIS723 4.1 74.8 1.0 HB3 B:ASP653 4.1 76.8 1.0 O B:ASP653 4.2 76.8 1.0 ND1 B:HIS723 4.2 74.8 1.0 CD2 B:HIS737 4.2 79.0 1.0 CG B:HIS737 4.2 79.0 1.0 HB2 B:ASP653 4.3 76.8 1.0 C6N B:NAD902 4.3 83.8 1.0 HG1 B:THR656 4.5 74.9 1.0 HA B:ASP653 4.5 76.8 1.0 HD1 B:HIS657 4.5 73.9 1.0 H6N B:NAD902 4.6 83.8 1.0 HD11 B:LEU719 4.6 74.3 1.0 CA B:ASP653 4.6 76.8 1.0 C B:ASP653 4.6 76.8 1.0 CG B:ASN741 4.7 77.4 1.0 HA B:THR601 4.7 79.5 1.0 OG1 B:THR656 4.7 74.9 1.0 HG B:LEU719 4.8 74.3 1.0 C3N B:NAD902 4.9 83.8 1.0 HD1 B:HIS723 4.9 74.8 1.0 HE2 B:HIS727 5.0 79.6 1.0

P.Pony, C.Rapisarda, L.Terradot, E.Marza, R.Fronzes. Filamentation of the Bacterial Bi-Functional Alcohol/Aldehyde Dehydrogenase Adhe Is Essential For Substrate Channeling and Enzymatic Regulation. Nat Commun V. 11 1426 2020.
ISSN: ESSN 2041-1723
PubMed: 32188856
DOI: 10.1038/S41467-020-15214-Y