Iron in PDB 1mnh: 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: 1mnh was solved by G.J.Davies, A.J.Wilkinson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.30
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	29.700, 119.510, 58.180, 90.00, 90.00, 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 1mnh). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was 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: 1mnh:

Iron binding site 1 out of 1 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:15.9 occ:1.00 FE A:HEM154 0.0 15.9 1.0 NC A:HEM154 2.0 15.8 1.0 ND A:HEM154 2.0 12.1 1.0 NB A:HEM154 2.0 13.3 1.0 NA A:HEM154 2.1 20.7 1.0 NE2 A:HIS93 2.2 12.8 1.0 C4B A:HEM154 3.0 8.0 1.0 C1D A:HEM154 3.1 11.3 1.0 C4D A:HEM154 3.1 10.8 1.0 C1C A:HEM154 3.1 8.4 1.0 C4A A:HEM154 3.1 14.0 1.0 C4C A:HEM154 3.1 9.8 1.0 C1A A:HEM154 3.1 15.7 1.0 CE1 A:HIS93 3.1 17.0 1.0 C1B A:HEM154 3.1 7.9 1.0 CD2 A:HIS93 3.2 11.7 1.0 CHC A:HEM154 3.4 10.2 1.0 CHD A:HEM154 3.5 8.2 1.0 CHA A:HEM154 3.5 14.7 1.0 CHB A:HEM154 3.5 9.1 1.0 CG2 A:VAL68 4.1 9.6 1.0 ND1 A:HIS93 4.2 14.7 1.0 C3A A:HEM154 4.3 13.6 1.0 C3D A:HEM154 4.3 18.6 1.0 C2A A:HEM154 4.3 16.7 1.0 C3B A:HEM154 4.3 9.0 1.0 C2D A:HEM154 4.3 13.9 1.0 C3C A:HEM154 4.3 13.4 1.0 C2C A:HEM154 4.3 13.2 1.0 CG A:HIS93 4.3 18.8 1.0 C2B A:HEM154 4.3 6.9 1.0 CD2 A: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