Manganese in PDB 4it2: Mn(III)-Ppix Bound Tt H-Nox

The structure of Mn(III)-Ppix Bound Tt H-Nox, PDB code: 4it2 was solved by M.B.Winter, P.J.Klemm, C.M.Phillips-Piro, K.M.Raymond, M.A.Marletta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	33.89 / 2.10
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	120.245, 45.416, 95.743, 90.00, 122.82, 90.00
R / Rfree (%)	20.9 / 24.5

The binding sites of Manganese atom in the Mn(III)-Ppix Bound Tt H-Nox (pdb code 4it2). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total 3 binding sites of Manganese where determined in the Mn(III)-Ppix Bound Tt H-Nox, PDB code: 4it2:
Jump to Manganese binding site number: 1; 2; 3;

Manganese binding site 1 out of 3 in the Mn(III)-Ppix Bound Tt H-Nox


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Mn(III)-Ppix Bound Tt H-Nox within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn500 b:41.0 occ:0.95 MN A:MNH500 0.0 41.0 0.9 NB A:MNH500 2.1 49.3 0.9 NC A:MNH500 2.1 42.4 0.9 NA A:MNH500 2.1 45.5 0.9 ND A:MNH500 2.2 45.1 0.9 NE2 A:HIS102 2.5 43.5 0.7 CE1 A:HIS102 2.8 46.5 0.7 C4C A:MNH500 3.0 39.7 0.9 C1B A:MNH500 3.0 44.4 0.9 C4A A:MNH500 3.0 51.3 0.9 C1D A:MNH500 3.1 42.9 0.9 C4B A:MNH500 3.1 45.0 0.9 C1C A:MNH500 3.1 41.7 0.9 C1A A:MNH500 3.2 48.9 0.9 C4D A:MNH500 3.2 45.8 0.9 CHD A:MNH500 3.3 36.9 0.9 CHB A:MNH500 3.3 49.3 0.9 CHC A:MNH500 3.5 42.6 0.9 CHA A:MNH500 3.6 41.8 0.9 CD2 A:HIS102 3.7 47.4 0.7 ND1 A:HIS102 4.0 47.0 0.7 C3C A:MNH500 4.2 34.6 0.9 C2B A:MNH500 4.3 46.8 0.9 C3A A:MNH500 4.3 54.2 0.9 C2C A:MNH500 4.3 35.9 0.9 C3B A:MNH500 4.3 52.4 0.9 C2A A:MNH500 4.3 47.0 0.9 C2D A:MNH500 4.4 44.9 0.9 C3D A:MNH500 4.4 43.2 0.9 CG A:HIS102 4.5 48.0 0.7 CE2 A:PHE78 4.9 46.2 1.0 CD1 A:LEU144 5.0 34.6 1.0

Manganese binding site 2 out of 3 in the Mn(III)-Ppix Bound Tt H-Nox


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 2 of Mn(III)-Ppix Bound Tt H-Nox within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn201 b:33.5 occ:0.98 MN B:MNH201 0.0 33.5 1.0 NC B:MNH201 2.0 32.9 1.0 NA B:MNH201 2.1 34.2 1.0 NB B:MNH201 2.1 40.4 1.0 ND B:MNH201 2.2 34.5 1.0 NE2 B:HIS102 2.5 41.2 1.0 O B:HOH325 2.9 41.0 1.0 C4C B:MNH201 3.0 35.3 1.0 C4A B:MNH201 3.1 37.7 1.0 CE1 B:HIS102 3.1 42.3 1.0 C1B B:MNH201 3.1 36.8 1.0 C1C B:MNH201 3.1 41.8 1.0 C1D B:MNH201 3.1 31.0 1.0 C4B B:MNH201 3.1 37.8 1.0 C1A B:MNH201 3.1 34.9 1.0 C4D B:MNH201 3.2 33.6 1.0 CHD B:MNH201 3.3 31.5 1.0 CHB B:MNH201 3.4 34.9 1.0 CHC B:MNH201 3.5 37.4 1.0 CHA B:MNH201 3.6 31.5 1.0 CD2 B:HIS102 3.6 39.2 1.0 C3C B:MNH201 4.2 31.2 1.0 C2C B:MNH201 4.3 38.2 1.0 C3A B:MNH201 4.3 36.2 1.0 ND1 B:HIS102 4.3 44.6 1.0 C2B B:MNH201 4.3 41.6 1.0 C2A B:MNH201 4.3 32.5 1.0 C3B B:MNH201 4.3 40.5 1.0 C2D B:MNH201 4.4 31.2 1.0 C3D B:MNH201 4.4 29.8 1.0 CG B:HIS102 4.6 40.4 1.0 CE2 B:PHE78 5.0 40.0 1.0

Manganese binding site 3 out of 3 in the Mn(III)-Ppix Bound Tt H-Nox


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 3 of Mn(III)-Ppix Bound Tt H-Nox within 5.0Å range: probe atom residue distance (Å) B Occ B:Mn202 b:42.8 occ:0.37 MN B:MNH202 0.0 42.8 0.4 NC B:MNH202 2.1 45.4 0.4 NB B:MNH202 2.1 45.4 0.4 ND B:MNH202 2.1 45.7 0.4 NA B:MNH202 2.1 45.5 0.4 O B:PRO121 2.6 41.3 1.0 C1D B:MNH202 3.0 46.3 0.4 C4C B:MNH202 3.0 45.7 0.4 C1B B:MNH202 3.1 45.9 0.4 C4A B:MNH202 3.1 46.0 0.4 C1C B:MNH202 3.1 46.0 0.4 C4B B:MNH202 3.1 46.0 0.4 C1A B:MNH202 3.2 46.0 0.4 C4D B:MNH202 3.2 45.9 0.4 CHD B:MNH202 3.4 45.3 0.4 CHB B:MNH202 3.4 45.9 0.4 CHC B:MNH202 3.5 47.4 0.4 CHA B:MNH202 3.5 46.4 0.4 C B:PRO121 3.6 45.3 1.0 CB B:PRO121 4.2 43.2 1.0 C3C B:MNH202 4.3 46.2 0.4 C2C B:MNH202 4.3 47.3 0.4 C2D B:MNH202 4.3 47.0 0.4 C2B B:MNH202 4.3 45.4 0.4 C3B B:MNH202 4.3 47.1 0.4 C3A B:MNH202 4.3 46.8 0.4 C3D B:MNH202 4.4 46.8 0.4 C2A B:MNH202 4.4 46.6 0.4 N B:VAL122 4.4 40.6 1.0 CA B:PRO121 4.4 43.1 1.0 CA B:VAL122 4.5 44.2 1.0 N B:PRO121 4.5 43.5 1.0 CD B:PRO121 4.6 43.4 1.0 CG B:PRO121 4.9 45.2 1.0

M.B.Winter, P.J.Klemm, C.M.Phillips-Piro, K.N.Raymond, M.A.Marletta. Porphyrin-Substituted H-Nox Proteins As High-Relaxivity Mri Contrast Agents. Inorg.Chem. V. 52 2277 2013.
ISSN: ISSN 0020-1669
PubMed: 23394479
DOI: 10.1021/IC302685H