Manganese in PDB 2o5b: Manganese Horse Heart Myoglobin, Reduced

The structure of Manganese Horse Heart Myoglobin, Reduced, PDB code: 2o5b was solved by G.B.Richter-Addo, Z.N.Zahran, L.Chooback, D.M.Copeland, A.H.West, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.63 / 2.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	35.207, 28.741, 64.201, 90.00, 105.45, 90.00
R / Rfree (%)	19.4 / 23.9

The binding sites of Manganese atom in the Manganese Horse Heart Myoglobin, Reduced (pdb code 2o5b). This binding sites where shown within 5.0 Angstroms radius around Manganese atom.
In total only one binding site of Manganese was determined in the Manganese Horse Heart Myoglobin, Reduced, PDB code: 2o5b:

Manganese binding site 1 out of 1 in the Manganese Horse Heart Myoglobin, Reduced


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of Manganese Horse Heart Myoglobin, Reduced within 5.0Å range: probe atom residue distance (Å) B Occ X:Mn154 b:24.9 occ:1.00 MN X:MNH154 0.0 24.9 1.0 NC X:MNH154 2.0 24.1 1.0 NB X:MNH154 2.1 27.1 1.0 NA X:MNH154 2.1 24.6 1.0 ND X:MNH154 2.1 25.1 1.0 NE2 X:HIS93 2.3 27.8 1.0 C4B X:MNH154 2.9 27.7 1.0 C1C X:MNH154 2.9 23.7 1.0 C4C X:MNH154 3.0 23.1 1.0 C4A X:MNH154 3.1 24.3 1.0 C1B X:MNH154 3.1 25.6 1.0 C1D X:MNH154 3.1 21.0 1.0 C1A X:MNH154 3.1 19.0 1.0 CD2 X:HIS93 3.2 24.6 1.0 C4D X:MNH154 3.2 22.8 1.0 CE1 X:HIS93 3.3 26.6 1.0 CHC X:MNH154 3.3 25.4 1.0 CHD X:MNH154 3.5 21.7 1.0 CHB X:MNH154 3.6 24.9 1.0 CHA X:MNH154 3.7 22.3 1.0 C3B X:MNH154 4.2 23.3 1.0 C3C X:MNH154 4.2 26.0 1.0 O X:HOH160 4.2 8.8 0.3 C2C X:MNH154 4.2 26.3 1.0 C2B X:MNH154 4.3 25.1 1.0 C2A X:MNH154 4.3 24.3 1.0 CG X:HIS93 4.4 26.1 1.0 ND1 X:HIS93 4.4 27.5 1.0 C3A X:MNH154 4.4 22.8 1.0 NE2 X:HIS64 4.4 31.9 1.0 C2D X:MNH154 4.5 22.7 1.0 C3D X:MNH154 4.6 25.8 1.0 CG2 X:VAL68 4.6 23.8 1.0 CE1 X:HIS64 4.6 27.8 1.0

Z.N.Zahran, L.Chooback, D.M.Copeland, A.H.West, G.B.Richter-Addo. Crystal Structures of Manganese- and Cobalt-Substituted Myoglobin in Complex with No and Nitrite Reveal Unusual Ligand Conformations. J.Inorg.Biochem. V. 102 216 2008.
ISSN: ISSN 0162-0134
PubMed: 17905436
DOI: 10.1016/J.JINORGBIO.2007.08.002