Iron in PDB 1mdn: Wild Type Myoglobin with Co

The structure of Wild Type Myoglobin with Co, PDB code: 1mdn 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 / 1.98
Space group	I 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	122.000, 42.170, 91.500, 90.00, 92.73, 90.00
R / Rfree (%)	19.8 / 26.2

The binding sites of Iron atom in the Wild Type Myoglobin with Co (pdb code 1mdn). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Wild Type Myoglobin with Co, PDB code: 1mdn:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Wild Type 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 Wild Type Myoglobin with Co within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe154 b:24.5 occ:1.00 FE A:HEM154 0.0 24.5 1.0 NA A:HEM154 2.0 19.2 1.0 NC A:HEM154 2.0 23.4 1.0 NB A:HEM154 2.0 20.5 1.0 ND A:HEM154 2.0 24.2 1.0 NE2 A:HIS93 2.2 23.4 1.0 C4B A:HEM154 3.0 17.4 1.0 C1B A:HEM154 3.0 17.5 1.0 C1A A:HEM154 3.0 23.4 1.0 C4A A:HEM154 3.0 20.7 1.0 C4D A:HEM154 3.0 25.4 1.0 C1C A:HEM154 3.1 22.4 1.0 C4C A:HEM154 3.1 24.8 1.0 C1D A:HEM154 3.1 27.5 1.0 CD2 A:HIS93 3.1 22.2 1.0 CE1 A:HIS93 3.2 20.4 1.0 CHB A:HEM154 3.4 17.3 1.0 CHA A:HEM154 3.4 23.8 1.0 CHC A:HEM154 3.4 23.1 1.0 CHD A:HEM154 3.5 26.1 1.0 C2A A:HEM154 4.2 20.4 1.0 C3A A:HEM154 4.2 19.8 1.0 ND1 A:HIS93 4.3 23.1 1.0 C2B A:HEM154 4.3 15.8 1.0 C3B A:HEM154 4.3 18.7 1.0 CG A:HIS93 4.3 23.2 1.0 C3D A:HEM154 4.3 27.4 1.0 C3C A:HEM154 4.3 29.4 1.0 C2C A:HEM154 4.3 26.2 1.0 C2D A:HEM154 4.3 26.9 1.0 NE2 A:HIS64 4.3 26.4 1.0 ND2 A:ASN68 4.5 29.2 1.0 CE1 A:HIS64 4.6 33.5 1.0 CD2 A:HIS97 4.9 25.3 1.0

Iron binding site 2 out of 2 in the Wild Type 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 Wild Type Myoglobin with Co within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe154 b:24.6 occ:1.00 FE B:HEM154 0.0 24.6 1.0 NA B:HEM154 1.9 16.3 1.0 NC B:HEM154 2.0 22.5 1.0 NB B:HEM154 2.1 18.9 1.0 ND B:HEM154 2.1 22.7 1.0 NE2 B:HIS93 2.2 23.9 1.0 O B:HOH352 3.0 41.6 1.0 C4A B:HEM154 3.0 20.8 1.0 C1A B:HEM154 3.0 24.6 1.0 CE1 B:HIS93 3.0 19.9 1.0 C4B B:HEM154 3.0 15.8 1.0 C4C B:HEM154 3.0 19.7 1.0 C1B B:HEM154 3.0 15.2 1.0 C4D B:HEM154 3.1 22.0 1.0 C1C B:HEM154 3.1 21.8 1.0 C1D B:HEM154 3.1 23.0 1.0 CD2 B:HIS93 3.2 18.9 1.0 CHB B:HEM154 3.4 18.7 1.0 CHD B:HEM154 3.4 21.9 1.0 CHC B:HEM154 3.4 20.6 1.0 CHA B:HEM154 3.4 21.8 1.0 ND1 B:HIS93 4.2 24.2 1.0 C2A B:HEM154 4.2 17.2 1.0 C3A B:HEM154 4.2 20.0 1.0 C3C B:HEM154 4.3 23.9 1.0 C2C B:HEM154 4.3 20.1 1.0 CG B:HIS93 4.3 22.5 1.0 C3D B:HEM154 4.3 25.0 1.0 C3B B:HEM154 4.3 19.2 1.0 C2B B:HEM154 4.3 15.9 1.0 C2D B:HEM154 4.3 26.4 1.0 NE2 B:HIS64 4.3 31.0 1.0 CE1 B:HIS64 4.5 33.6 1.0 ND2 B:ASN68 4.7 28.5 1.0 CD2 B:HIS97 4.9 27.9 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