Iron in PDB 1do3: Carbonmonoxy-Myoglobin (Mutant L29W) After Photolysis at T>180K

The structure of Carbonmonoxy-Myoglobin (Mutant L29W) After Photolysis at T>180K, PDB code: 1do3 was solved by A.Ostermann, R.Waschipky, F.G.Parak, G.U.Nienhaus, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	7.00 / 1.55
Space group	P 6
Cell size a, b, c (Å), α, β, γ (°)	90.460, 90.460, 45.260, 90.00, 90.00, 120.00
R / Rfree (%)	19.3 / 21.8

The binding sites of Iron atom in the Carbonmonoxy-Myoglobin (Mutant L29W) After Photolysis at T>180K (pdb code 1do3). 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 Carbonmonoxy-Myoglobin (Mutant L29W) After Photolysis at T>180K, PDB code: 1do3:

Iron binding site 1 out of 1 in the Carbonmonoxy-Myoglobin (Mutant L29W) After Photolysis at T>180K


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Carbonmonoxy-Myoglobin (Mutant L29W) After Photolysis at T>180K within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe154 b:7.4 occ:1.00 FE A:HEM154 0.0 7.4 1.0 ND A:HEM154 2.0 6.5 1.0 NC A:HEM154 2.0 6.4 1.0 NA A:HEM154 2.0 7.4 1.0 NB A:HEM154 2.0 7.0 1.0 NE2 A:HIS93 2.2 5.0 1.0 C1D A:HEM154 3.0 6.6 1.0 C4D A:HEM154 3.0 6.2 1.0 C4C A:HEM154 3.0 5.8 1.0 C1A A:HEM154 3.1 6.0 1.0 C4A A:HEM154 3.1 6.7 1.0 C1C A:HEM154 3.1 5.5 1.0 C1B A:HEM154 3.1 6.5 1.0 C4B A:HEM154 3.1 6.3 1.0 CE1 A:HIS93 3.1 6.6 1.0 CD2 A:HIS93 3.2 5.5 1.0 CHD A:HEM154 3.4 6.3 1.0 CHA A:HEM154 3.4 6.4 1.0 CHB A:HEM154 3.4 7.0 1.0 CHC A:HEM154 3.5 6.2 1.0 C3D A:HEM154 4.2 7.7 1.0 C2D A:HEM154 4.2 7.1 1.0 ND1 A:HIS93 4.3 5.7 1.0 C3C A:HEM154 4.3 6.2 1.0 C2C A:HEM154 4.3 5.0 1.0 C2A A:HEM154 4.3 6.1 1.0 C3A A:HEM154 4.3 5.5 1.0 CG A:HIS93 4.3 4.6 1.0 C2B A:HEM154 4.4 6.7 1.0 C3B A:HEM154 4.4 7.7 1.0 CE1 A:HIS64 4.5 11.2 1.0 CG2 A:VAL68 4.5 3.6 1.0 CH2 A:TRP29 4.9 15.4 1.0 CD2 A:HIS97 5.0 8.7 1.0 NE2 A:HIS64 5.0 11.9 1.0 O A:CMO155 5.0 16.0 0.6

A.Ostermann, R.Waschipky, F.G.Parak, G.U.Nienhaus. Ligand Binding and Conformational Motions in Myoglobin. Nature V. 404 205 2000.
ISSN: ISSN 0028-0836
PubMed: 10724176
DOI: 10.1038/35004622