Manganese in PDB 1nz5: The Horse Heart Myoglobin Variant K45E/K63E Complexed with Manganese

The structure of The Horse Heart Myoglobin Variant K45E/K63E Complexed with Manganese, PDB code: 1nz5 was solved by C.L.Hunter, R.Maurus, M.R.Mauk, H.Lee, E.L.Raven, H.Tong, N.Nguyen, S.Smith, G.D.Brayer, A.G.Mauk, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.70
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	28.900, 35.600, 125.100, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The structure of The Horse Heart Myoglobin Variant K45E/K63E Complexed with Manganese also contains other interesting chemical elements:

Iron

(Fe)

1 atom

The binding sites of Manganese atom in the The Horse Heart Myoglobin Variant K45E/K63E Complexed with Manganese (pdb code 1nz5). 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 The Horse Heart Myoglobin Variant K45E/K63E Complexed with Manganese, PDB code: 1nz5:

Manganese binding site 1 out of 1 in the The Horse Heart Myoglobin Variant K45E/K63E Complexed with Manganese


Mono view


Stereo pair view

A full contact list of Manganese with other atoms in the Mn binding site number 1 of The Horse Heart Myoglobin Variant K45E/K63E Complexed with Manganese within 5.0Å range: probe atom residue distance (Å) B Occ A:Mn300 b:43.8 occ:1.00 O A:HOH298 2.2 44.4 1.0 O2D A:HEM154 2.3 26.3 1.0 OE1 A:GLU45 2.5 48.9 1.0 O A:HOH299 2.9 59.3 1.0 CGD A:HEM154 2.9 25.0 1.0 O1D A:HEM154 3.0 28.2 1.0 OE2 A:GLU45 3.0 51.1 1.0 CD A:GLU45 3.0 46.4 1.0 CBD A:HEM154 4.3 21.7 1.0 O A:HOH214 4.3 45.2 1.0 O A:HOH171 4.5 36.1 1.0 CG A:GLU45 4.5 39.8 1.0

C.L.Hunter, R.Maurus, M.R.Mauk, H.Lee, E.L.Raven, H.Tong, N.Nguyen, S.Smith, G.D.Brayer, A.G.Mauk. Introduction and Characterization of A Functionally Linked Metal Ion Binding Site at the Exposed Heme Edge of Myoglobin Proc.Natl.Acad.Sci.Usa V. 100 3647 2003.
ISSN: ISSN 0027-8424
PubMed: 12644706
DOI: 10.1073/PNAS.0636702100