Manganese in PDB 7w7a: Heme Exporter in Complex with Mn-Containing Protoporphyrin IX, Mn- Anomalous Data

The structure of Heme Exporter in Complex with Mn-Containing Protoporphyrin IX, Mn- Anomalous Data, PDB code: 7w7a was solved by T.Hisano, H.Nakamura, M.M.Rahman, T.Tosha, M.Shirouzu, Y.Shiro, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.82 / 3.20
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	82.488, 133.672, 159.838, 111.81, 99.83, 94.43
R / Rfree (%)	26.4 / 30.3

The binding sites of Manganese atom in the Heme Exporter in Complex with Mn-Containing Protoporphyrin IX, Mn- Anomalous Data (pdb code 7w7a). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Heme Exporter in Complex with Mn-Containing Protoporphyrin IX, Mn- Anomalous Data, PDB code: 7w7a:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Heme Exporter in Complex with Mn-Containing Protoporphyrin IX, Mn- Anomalous Data


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Heme Exporter in Complex with Mn-Containing Protoporphyrin IX, Mn- Anomalous Data within 5.0Å range: probe atom residue distance (Å) B Occ D:Mn401 b:240.4 occ:1.00 MN D:MNR401 0.0 240.4 1.0 OE2 B:GLU219 1.9 124.7 1.0 OE2 D:GLU219 1.9 144.7 1.0 NB D:MNR401 2.1 239.6 1.0 ND D:MNR401 2.1 241.4 1.0 NC D:MNR401 2.1 239.8 1.0 NA D:MNR401 2.1 241.1 1.0 C4C D:MNR401 3.1 240.0 1.0 C1D D:MNR401 3.1 241.4 1.0 C1A D:MNR401 3.1 241.9 1.0 C4D D:MNR401 3.1 242.1 1.0 C4A D:MNR401 3.1 241.0 1.0 C1C D:MNR401 3.1 239.1 1.0 CD B:GLU219 3.2 124.4 1.0 C1B D:MNR401 3.2 239.6 1.0 C4B D:MNR401 3.2 238.8 1.0 CD D:GLU219 3.2 146.1 1.0 CHD D:MNR401 3.4 240.8 1.0 CHA D:MNR401 3.5 242.3 1.0 CHB D:MNR401 3.5 240.2 1.0 CHC D:MNR401 3.5 238.6 1.0 OE1 B:GLU219 3.9 124.8 1.0 OE1 D:GLU219 4.0 148.7 1.0 CG D:GLU219 4.1 144.6 1.0 CG B:GLU219 4.2 123.4 1.0 C3C D:MNR401 4.4 239.4 1.0 C2A D:MNR401 4.4 242.2 1.0 C3D D:MNR401 4.4 242.6 1.0 C2D D:MNR401 4.4 242.2 1.0 C3A D:MNR401 4.4 241.6 1.0 C2C D:MNR401 4.4 238.8 1.0 C3B D:MNR401 4.5 238.4 1.0 C2B D:MNR401 4.5 238.9 1.0 NE2 D:HIS163 4.6 154.1 1.0 CB D:GLU219 4.8 145.1 1.0 CB B:GLU219 4.8 123.8 1.0 CD1 D:LEU39 4.8 183.1 1.0 CE1 D:HIS163 4.8 153.5 1.0 CE1 B:HIS163 4.9 119.3 1.0 NE2 B:HIS163 5.0 119.6 1.0

Manganese binding site 2 out of 2 in the Heme Exporter in Complex with Mn-Containing Protoporphyrin IX, Mn- Anomalous Data


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Heme Exporter in Complex with Mn-Containing Protoporphyrin IX, Mn- Anomalous Data within 5.0Å range: probe atom residue distance (Å) B Occ H:Mn401 b:482.5 occ:1.00 MN H:MNR401 0.0 482.5 1.0 OE2 F:GLU219 1.9 149.9 1.0 OE2 H:GLU219 1.9 161.3 1.0 NB H:MNR401 2.1 483.2 1.0 ND H:MNR401 2.1 481.7 1.0 NA H:MNR401 2.1 482.1 1.0 NC H:MNR401 2.1 482.9 1.0 C4C H:MNR401 3.1 482.9 1.0 C1A H:MNR401 3.1 481.4 1.0 C1D H:MNR401 3.1 481.9 1.0 C4D H:MNR401 3.1 481.1 1.0 C4A H:MNR401 3.1 482.6 1.0 C1C H:MNR401 3.1 483.3 1.0 C4B H:MNR401 3.1 483.7 1.0 C1B H:MNR401 3.2 483.6 1.0 CD H:GLU219 3.2 160.5 1.0 CD F:GLU219 3.2 148.0 1.0 CHA H:MNR401 3.4 480.8 1.0 CHD H:MNR401 3.4 482.5 1.0 CHC H:MNR401 3.5 483.6 1.0 CHB H:MNR401 3.5 483.4 1.0 OE1 F:GLU219 4.0 148.4 1.0 OE1 H:GLU219 4.0 161.4 1.0 CG H:GLU219 4.1 158.6 1.0 CG F:GLU219 4.2 145.0 1.0 C3C H:MNR401 4.4 483.3 1.0 C2D H:MNR401 4.4 481.3 1.0 C2A H:MNR401 4.4 481.4 1.0 C3D H:MNR401 4.4 480.7 1.0 C3A H:MNR401 4.4 482.2 1.0 C3B H:MNR401 4.4 484.4 1.0 C2C H:MNR401 4.4 483.6 1.0 C2B H:MNR401 4.4 484.3 1.0 NE2 F:HIS163 4.6 133.7 1.0 NE2 H:HIS163 4.7 172.5 1.0 CE1 H:HIS163 4.7 175.0 1.0 CB F:GLU219 4.9 145.1 1.0 CB H:GLU219 4.9 158.5 1.0 CE1 F:HIS163 4.9 133.6 1.0

H.Nakamura, T.Hisano, M.M.Rahman, T.Tosha, M.Shirouzu, Y.Shiro. Structural Basis For Heme Detoxification By An Atp-Binding Cassette-Type Efflux Pump in Gram-Positive Pathogenic Bacteria. Proc.Natl.Acad.Sci.Usa V. 119 85119 2022.
ISSN: ESSN 1091-6490
PubMed: 35767641
DOI: 10.1073/PNAS.2123385119