Iron in PDB 1mnj: Interactions Among Residues CD3, E7, E10 and E11 in Myoglobins: Attempts to Simulate the O2 and Co Binding Properties of Aplysia Myoglobin

The structure of Interactions Among Residues CD3, E7, E10 and E11 in Myoglobins: Attempts to Simulate the O2 and Co Binding Properties of Aplysia Myoglobin, PDB code: 1mnj was solved by S.Krzywda, A.J.Wilkinson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.20
Space group	I 21
Cell size a, b, c (Å), α, β, γ (°)	124.290, 42.560, 92.450, 90.00, 92.65, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Iron atom in the Interactions Among Residues CD3, E7, E10 and E11 in Myoglobins: Attempts to Simulate the O2 and Co Binding Properties of Aplysia Myoglobin (pdb code 1mnj). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Interactions Among Residues CD3, E7, E10 and E11 in Myoglobins: Attempts to Simulate the O2 and Co Binding Properties of Aplysia Myoglobin, PDB code: 1mnj:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Interactions Among Residues CD3, E7, E10 and E11 in Myoglobins: Attempts to Simulate the O2 and Co Binding Properties of Aplysia Myoglobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Interactions Among Residues CD3, E7, E10 and E11 in Myoglobins: Attempts to Simulate the O2 and Co Binding Properties of Aplysia Myoglobin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe154 b:20.0 occ:1.00 FE A:HEM154 0.0 20.0 1.0 NC A:HEM154 2.0 18.3 1.0 NA A:HEM154 2.0 18.1 1.0 ND A:HEM154 2.1 19.9 1.0 NB A:HEM154 2.1 17.4 1.0 NE2 A:HIS93 2.2 20.2 1.0 C4A A:HEM154 3.0 18.1 1.0 C4C A:HEM154 3.0 18.9 1.0 C1C A:HEM154 3.1 18.4 1.0 C1A A:HEM154 3.1 19.4 1.0 C1D A:HEM154 3.1 20.1 1.0 C4B A:HEM154 3.1 16.7 1.0 C1B A:HEM154 3.1 16.2 1.0 CD2 A:HIS93 3.1 19.8 1.0 C4D A:HEM154 3.1 20.3 1.0 CE1 A:HIS93 3.2 22.0 1.0 CHB A:HEM154 3.4 16.8 1.0 CHD A:HEM154 3.4 19.1 1.0 CHC A:HEM154 3.5 17.0 1.0 CHA A:HEM154 3.5 19.5 1.0 CG1 A:ILE68 4.2 17.4 1.0 CD1 A:ILE68 4.2 18.0 1.0 CG A:HIS93 4.2 23.0 1.0 C3A A:HEM154 4.2 18.1 1.0 ND1 A:HIS93 4.2 21.9 1.0 C2A A:HEM154 4.3 19.5 1.0 C3C A:HEM154 4.3 19.0 1.0 C3D A:HEM154 4.3 20.9 1.0 C2C A:HEM154 4.3 18.6 1.0 C3B A:HEM154 4.3 16.5 1.0 C2D A:HEM154 4.3 20.7 1.0 C2B A:HEM154 4.3 16.2 1.0

Iron binding site 2 out of 2 in the Interactions Among Residues CD3, E7, E10 and E11 in Myoglobins: Attempts to Simulate the O2 and Co Binding Properties of Aplysia Myoglobin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Interactions Among Residues CD3, E7, E10 and E11 in Myoglobins: Attempts to Simulate the O2 and Co Binding Properties of Aplysia Myoglobin within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe154 b:19.7 occ:1.00 FE B:HEM154 0.0 19.7 1.0 NC B:HEM154 2.0 17.6 1.0 NB B:HEM154 2.0 17.5 1.0 NA B:HEM154 2.0 18.4 1.0 ND B:HEM154 2.1 19.5 1.0 NE2 B:HIS93 2.2 19.3 1.0 C1C B:HEM154 3.0 18.4 1.0 C4C B:HEM154 3.0 18.0 1.0 C1D B:HEM154 3.0 19.6 1.0 CD2 B:HIS93 3.0 21.5 1.0 C4B B:HEM154 3.1 17.6 1.0 C4A B:HEM154 3.1 18.3 1.0 C4D B:HEM154 3.1 20.2 1.0 C1B B:HEM154 3.1 17.0 1.0 C1A B:HEM154 3.1 19.4 1.0 CE1 B:HIS93 3.2 20.9 1.0 CHC B:HEM154 3.4 17.6 1.0 CHD B:HEM154 3.5 18.5 1.0 CHB B:HEM154 3.5 17.0 1.0 CHA B:HEM154 3.6 19.4 1.0 CD1 B:ILE68 4.2 11.6 1.0 CG B:HIS93 4.2 25.3 1.0 C3C B:HEM154 4.2 18.1 1.0 C2C B:HEM154 4.3 18.1 1.0 C3D B:HEM154 4.3 21.4 1.0 ND1 B:HIS93 4.3 24.2 1.0 C2D B:HEM154 4.3 21.0 1.0 CG1 B:ILE68 4.3 14.3 1.0 C2B B:HEM154 4.3 17.2 1.0 C3B B:HEM154 4.3 17.5 1.0 C3A B:HEM154 4.3 18.3 1.0 C2A B:HEM154 4.3 19.2 1.0 CD2 B:HIS97 4.9 22.1 1.0

S.J.Smerdon, S.Krzywda, A.M.Brzozowski, G.J.Davies, A.J.Wilkinson, A.Brancaccio, F.Cutruzzola, C.T.Allocatelli, M.Brunori, T.Li, R.E.Brantley Jr., T.E.Carver, R.F.Eich, E.Singleton, J.S.Olson. Interactions Among Residues CD3, E7, E10, and E11 in Myoglobins: Attempts to Simulate the Ligand-Binding Properties of Aplysia Myoglobin. Biochemistry V. 34 8715 1995.
ISSN: ISSN 0006-2960
PubMed: 7612611
DOI: 10.1021/BI00027A022