Manganese in PDB 3quh: Structure of Heme Transport Protein Isdh-NEAT3 From S. Aureus in Complex with Manganese(III)-Porphyrin

The structure of Structure of Heme Transport Protein Isdh-NEAT3 From S. Aureus in Complex with Manganese(III)-Porphyrin, PDB code: 3quh was solved by Y.Moriwaki, J.M.M.Caaveiro, K.Tsumoto, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.14 / 2.70
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	41.280, 75.930, 49.330, 90.00, 95.09, 90.00
R / Rfree (%)	22.4 / 28.6

The binding sites of Manganese atom in the Structure of Heme Transport Protein Isdh-NEAT3 From S. Aureus in Complex with Manganese(III)-Porphyrin (pdb code 3quh). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Structure of Heme Transport Protein Isdh-NEAT3 From S. Aureus in Complex with Manganese(III)-Porphyrin, PDB code: 3quh:
Jump to Manganese binding site number: 1; 2;

Manganese binding site 1 out of 2 in the Structure of Heme Transport Protein Isdh-NEAT3 From S. Aureus in Complex with Manganese(III)-Porphyrin


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Structure of Heme Transport Protein Isdh-NEAT3 From S. Aureus in Complex with Manganese(III)-Porphyrin within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn3747 b:29.5 occ:1.00 MN A:MNR3747 0.0 29.5 1.0 NA A:MNR3747 2.1 30.6 1.0 NC A:MNR3747 2.1 26.1 1.0 ND A:MNR3747 2.1 28.9 1.0 NB A:MNR3747 2.1 28.8 1.0 OH A:TYR642 2.2 30.4 1.0 C1A A:MNR3747 3.1 31.6 1.0 C4A A:MNR3747 3.1 31.0 1.0 C4D A:MNR3747 3.1 30.1 1.0 C4C A:MNR3747 3.1 25.4 1.0 C1C A:MNR3747 3.1 25.1 1.0 C1D A:MNR3747 3.1 28.0 1.0 C4B A:MNR3747 3.1 26.7 1.0 C1B A:MNR3747 3.1 28.5 1.0 CZ A:TYR642 3.3 31.7 1.0 CHA A:MNR3747 3.4 30.9 1.0 CHB A:MNR3747 3.5 29.4 1.0 CHC A:MNR3747 3.5 25.0 1.0 CHD A:MNR3747 3.5 25.8 1.0 CG1 A:VAL564 3.7 31.8 1.0 CE2 A:TYR642 3.9 30.4 1.0 CE1 A:TYR642 4.1 32.7 1.0 OH A:TYR646 4.1 37.4 1.0 CB A:VAL564 4.3 32.4 1.0 C3A A:MNR3747 4.3 33.0 1.0 C2A A:MNR3747 4.3 34.0 1.0 C3C A:MNR3747 4.3 24.1 1.0 C2C A:MNR3747 4.3 24.5 1.0 C3D A:MNR3747 4.4 30.1 1.0 C2D A:MNR3747 4.4 28.3 1.0 C2B A:MNR3747 4.4 27.6 1.0 C3B A:MNR3747 4.4 26.1 1.0 CE1 A:TYR646 4.4 33.1 1.0 CZ A:TYR646 4.5 35.4 1.0 CG2 A:VAL564 4.7 33.7 1.0 CG2 A:VAL635 4.9 32.6 1.0

Manganese binding site 2 out of 2 in the Structure of Heme Transport Protein Isdh-NEAT3 From S. Aureus in Complex with Manganese(III)-Porphyrin


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Structure of Heme Transport Protein Isdh-NEAT3 From S. Aureus in Complex with Manganese(III)-Porphyrin within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn3747 b:29.0 occ:1.00 MN B:MNR3747 0.0 29.0 1.0 NC B:MNR3747 2.1 27.1 1.0 NA B:MNR3747 2.1 32.3 1.0 ND B:MNR3747 2.1 29.9 1.0 NB B:MNR3747 2.2 29.6 1.0 OH B:TYR642 2.3 30.0 1.0 C1C B:MNR3747 3.1 26.5 1.0 C1A B:MNR3747 3.1 33.7 1.0 C4C B:MNR3747 3.1 27.2 1.0 C4A B:MNR3747 3.1 32.7 1.0 C4D B:MNR3747 3.1 30.8 1.0 C1D B:MNR3747 3.1 29.0 1.0 C4B B:MNR3747 3.2 27.7 1.0 C1B B:MNR3747 3.2 29.8 1.0 CZ B:TYR642 3.4 31.1 1.0 CHA B:MNR3747 3.4 32.5 1.0 CHC B:MNR3747 3.5 26.4 1.0 CHD B:MNR3747 3.5 27.2 1.0 CHB B:MNR3747 3.5 31.1 1.0 CG1 B:VAL564 3.6 31.8 1.0 CE2 B:TYR642 4.0 30.0 1.0 OH B:TYR646 4.0 35.8 1.0 CE1 B:TYR646 4.3 32.5 1.0 C3C B:MNR3747 4.3 25.8 1.0 C2C B:MNR3747 4.3 26.6 1.0 C3A B:MNR3747 4.3 35.4 1.0 C2A B:MNR3747 4.3 36.7 1.0 CE1 B:TYR642 4.3 31.9 1.0 CB B:VAL564 4.4 32.8 1.0 C3D B:MNR3747 4.4 31.1 1.0 C2D B:MNR3747 4.4 29.7 1.0 C3B B:MNR3747 4.4 27.2 1.0 C2B B:MNR3747 4.4 28.8 1.0 CZ B:TYR646 4.4 34.3 1.0 CG2 B:VAL635 4.7 31.3 1.0 CG2 B:VAL564 4.9 34.0 1.0

Y.Moriwaki, J.M.M.Caaveiro, Y.Tanaka, H.Tsutsumi, I.Hamachi, K.Tsumoto. Molecular Basis of Recognition of Antibacterial Porphyrins By Heme-Transporter Isdh-NEAT3 of Staphylococcus Aureus. Biochemistry V. 50 7311 2011.
ISSN: ISSN 0006-2960
PubMed: 21797259
DOI: 10.1021/BI200493H