Iron in PDB 1m6c: V68N Myoglobin with Co

The structure of V68N Myoglobin with Co, PDB code: 1m6c 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 / 1.90
Space group	I 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	122.140, 42.300, 91.550, 90.00, 92.49, 90.00
R / Rfree (%)	19.2 / 26.1

The binding sites of Iron atom in the V68N Myoglobin with Co (pdb code 1m6c). 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 with Co, PDB code: 1m6c:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the V68N Myoglobin with Co


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of V68N Myoglobin with Co within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe154 b:23.9 occ:1.00 FE A:HEM154 0.0 23.9 1.0 C A:CMO155 1.8 21.8 1.0 NC A:HEM154 2.0 24.3 1.0 NB A:HEM154 2.0 19.4 1.0 NA A:HEM154 2.0 23.6 1.0 ND A:HEM154 2.1 22.9 1.0 NE2 A:HIS93 2.2 19.9 1.0 O A:CMO155 3.0 25.4 1.0 C4B A:HEM154 3.0 17.6 1.0 C1C A:HEM154 3.0 22.5 1.0 C1B A:HEM154 3.0 17.8 1.0 C1D A:HEM154 3.1 24.1 1.0 CD2 A:HIS93 3.1 17.8 1.0 C4C A:HEM154 3.1 22.6 1.0 C4D A:HEM154 3.1 22.0 1.0 C4A A:HEM154 3.1 22.4 1.0 C1A A:HEM154 3.1 22.1 1.0 CE1 A:HIS93 3.2 16.3 1.0 CHC A:HEM154 3.4 20.1 1.0 CHB A:HEM154 3.5 18.6 1.0 CHD A:HEM154 3.5 20.2 1.0 CHA A:HEM154 3.5 23.6 1.0 C3B A:HEM154 4.2 17.0 1.0 C2C A:HEM154 4.2 24.2 1.0 C2B A:HEM154 4.2 13.5 1.0 C3C A:HEM154 4.2 25.8 1.0 CG A:HIS93 4.3 21.9 1.0 ND1 A:HIS93 4.3 20.7 1.0 C3D A:HEM154 4.3 25.7 1.0 C2D A:HEM154 4.3 24.4 1.0 C2A A:HEM154 4.3 26.3 1.0 C3A A:HEM154 4.3 23.6 1.0 ND2 A:ASN68 4.5 20.2 1.0 O A:HOH374 4.8 39.9 1.0 CD2 A:HIS97 5.0 21.8 1.0

Iron binding site 2 out of 2 in the V68N Myoglobin with Co


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of V68N Myoglobin with Co within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe154 b:24.0 occ:1.00 FE B:HEM154 0.0 24.0 1.0 C B:CMO155 1.8 22.5 1.0 NA B:HEM154 1.8 16.4 1.0 NC B:HEM154 2.0 24.1 1.0 NB B:HEM154 2.1 18.7 1.0 ND B:HEM154 2.1 21.8 1.0 NE2 B:HIS93 2.2 18.3 1.0 C4A B:HEM154 2.9 22.9 1.0 O B:CMO155 3.0 24.1 1.0 CE1 B:HIS93 3.0 14.3 1.0 C1A B:HEM154 3.0 22.6 1.0 C4B B:HEM154 3.0 16.3 1.0 C1B B:HEM154 3.0 15.7 1.0 C4D B:HEM154 3.0 20.3 1.0 C1C B:HEM154 3.1 24.8 1.0 C1D B:HEM154 3.1 21.1 1.0 C4C B:HEM154 3.1 23.6 1.0 CD2 B:HIS93 3.2 19.0 1.0 CHA B:HEM154 3.4 24.1 1.0 CHB B:HEM154 3.4 19.4 1.0 CHC B:HEM154 3.4 19.2 1.0 CHD B:HEM154 3.5 23.5 1.0 C3A B:HEM154 4.1 23.0 1.0 C2A B:HEM154 4.2 23.0 1.0 ND1 B:HIS93 4.2 20.6 1.0 C2C B:HEM154 4.3 23.8 1.0 C2B B:HEM154 4.3 14.2 1.0 C3B B:HEM154 4.3 15.2 1.0 CG B:HIS93 4.3 19.8 1.0 C3D B:HEM154 4.3 23.4 1.0 C3C B:HEM154 4.3 27.5 1.0 C2D B:HEM154 4.3 23.5 1.0 ND2 B:ASN68 4.5 19.3 1.0 O B:HOH343 4.6 39.2 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