Iron in PDB 1mno: V68N Myoglobin Oxy Form

The structure of V68N Myoglobin Oxy Form, PDB code: 1mno was solved by G.N.Murshudov, S.Krzywda, A.M.Brzozowski, M.Jaskolski, E.E.Scott, S.A.Klizas, Q.H.Gibson, J.S.Olson, A.J.Wilkinson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.00 / 1.95
Space group	I 21
Cell size a, b, c (Å), α, β, γ (°)	122.180, 42.120, 91.560, 90.00, 92.62, 90.00
R / Rfree (%)	19.1 / 25

The binding sites of Iron atom in the V68N Myoglobin Oxy Form (pdb code 1mno). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the V68N Myoglobin Oxy Form, PDB code: 1mno:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the V68N Myoglobin Oxy Form


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of V68N Myoglobin Oxy Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe154 b:23.8 occ:1.00 FE A:HEM154 0.0 23.8 1.0 O1 A:OXY155 1.8 33.8 1.0 NC A:HEM154 2.0 21.2 1.0 NA A:HEM154 2.0 18.9 1.0 NB A:HEM154 2.0 20.6 1.0 ND A:HEM154 2.0 22.0 1.0 NE2 A:HIS93 2.2 24.1 1.0 O2 A:OXY155 2.7 46.3 1.0 C4C A:HEM154 3.0 24.4 1.0 C4B A:HEM154 3.0 16.0 1.0 C1C A:HEM154 3.0 21.9 1.0 C1B A:HEM154 3.0 17.6 1.0 C1D A:HEM154 3.0 26.2 1.0 C4A A:HEM154 3.1 21.5 1.0 C1A A:HEM154 3.1 20.0 1.0 C4D A:HEM154 3.1 23.0 1.0 CD2 A:HIS93 3.1 23.9 1.0 CE1 A:HIS93 3.2 19.6 1.0 CHD A:HEM154 3.4 24.8 1.0 CHB A:HEM154 3.4 18.4 1.0 CHC A:HEM154 3.5 16.4 1.0 CHA A:HEM154 3.5 21.8 1.0 C3C A:HEM154 4.2 26.2 1.0 C2C A:HEM154 4.2 24.2 1.0 ND1 A:HIS93 4.2 25.8 1.0 CG A:HIS93 4.3 26.8 1.0 C2B A:HEM154 4.3 16.7 1.0 C3B A:HEM154 4.3 18.6 1.0 C2A A:HEM154 4.3 19.4 1.0 NE2 A:HIS64 4.3 26.8 1.0 C3A A:HEM154 4.3 21.9 1.0 C3D A:HEM154 4.3 24.7 1.0 C2D A:HEM154 4.3 26.7 1.0 ND2 A:ASN68 4.4 25.4 1.0 CE1 A:HIS64 4.6 27.8 1.0

Iron binding site 2 out of 2 in the V68N Myoglobin Oxy Form


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of V68N Myoglobin Oxy Form within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe154 b:22.5 occ:1.00 FE B:HEM154 0.0 22.5 1.0 O1 B:OXY155 1.9 40.0 1.0 NA B:HEM154 1.9 17.5 1.0 NC B:HEM154 2.0 16.5 1.0 ND B:HEM154 2.1 19.6 1.0 NB B:HEM154 2.1 17.7 1.0 NE2 B:HIS93 2.2 22.9 1.0 O2 B:OXY155 2.8 47.3 1.0 C4A B:HEM154 3.0 19.9 1.0 C1A B:HEM154 3.0 22.5 1.0 C4D B:HEM154 3.0 19.0 1.0 C1B B:HEM154 3.0 17.4 1.0 C1D B:HEM154 3.0 21.9 1.0 C4C B:HEM154 3.0 19.1 1.0 C4B B:HEM154 3.0 14.9 1.0 CE1 B:HIS93 3.1 23.8 1.0 C1C B:HEM154 3.1 19.3 1.0 CD2 B:HIS93 3.2 20.6 1.0 CHB B:HEM154 3.4 16.1 1.0 CHA B:HEM154 3.4 17.2 1.0 CHD B:HEM154 3.4 19.0 1.0 CHC B:HEM154 3.5 18.7 1.0 C2A B:HEM154 4.2 16.8 1.0 C3A B:HEM154 4.2 19.4 1.0 ND1 B:HIS93 4.2 26.0 1.0 C3C B:HEM154 4.3 22.3 1.0 C2C B:HEM154 4.3 23.6 1.0 C3D B:HEM154 4.3 22.4 1.0 C2B B:HEM154 4.3 14.2 1.0 C3B B:HEM154 4.3 17.6 1.0 C2D B:HEM154 4.3 25.9 1.0 CG B:HIS93 4.3 25.2 1.0 NE2 B:HIS64 4.4 26.9 1.0 ND2 B:ASN68 4.5 24.0 1.0 CE1 B:HIS64 4.6 28.1 1.0

S.Krzywda, G.N.Murshudov, A.M.Brzozowski, M.Jaskolski, E.E.Scott, S.A.Klizas, Q.H.Gibson, J.S.Olson, A.J.Wilkinson. Stabilizing Bound O2 in Myoglobin By VALINE68 (E11) to Asparagine Substitution. Biochemistry V. 37 15896 1998.
ISSN: ISSN 0006-2960
PubMed: 9843395
DOI: 10.1021/BI9812470