Iron in PDB 1do1: Carbonmonoxy-Myoglobin Mutant L29W at 105K

The structure of Carbonmonoxy-Myoglobin Mutant L29W at 105K, PDB code: 1do1 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 / 1.50
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 (%)	18.9 / 21.5

The binding sites of Iron atom in the Carbonmonoxy-Myoglobin Mutant L29W at 105K (pdb code 1do1). 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 at 105K, PDB code: 1do1:

Iron binding site 1 out of 1 in the Carbonmonoxy-Myoglobin Mutant L29W at 105K


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 at 105K within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe154 b:7.0 occ:1.00 FE A:HEM154 0.0 7.0 1.0 C A:CMO155 1.8 9.5 1.0 ND A:HEM154 2.0 5.9 1.0 NC A:HEM154 2.0 6.0 1.0 NA A:HEM154 2.0 6.6 1.0 NB A:HEM154 2.0 6.7 1.0 NE2 A:HIS93 2.1 5.1 1.0 O A:CMO155 3.0 10.5 1.0 C1D A:HEM154 3.0 6.0 1.0 C4C A:HEM154 3.0 6.4 1.0 C4D A:HEM154 3.0 4.9 1.0 C1C A:HEM154 3.0 6.5 1.0 C1A A:HEM154 3.0 6.0 1.0 C4A A:HEM154 3.1 6.0 1.0 C4B A:HEM154 3.1 6.2 1.0 CE1 A:HIS93 3.1 7.9 1.0 C1B A:HEM154 3.1 6.7 1.0 CD2 A:HIS93 3.2 6.1 1.0 CHD A:HEM154 3.4 5.8 1.0 CHA A:HEM154 3.4 5.4 1.0 CHC A:HEM154 3.4 5.8 1.0 CHB A:HEM154 3.4 6.6 1.0 C3D A:HEM154 4.2 6.6 1.0 C2D A:HEM154 4.2 5.8 1.0 ND1 A:HIS93 4.2 6.7 1.0 C3C A:HEM154 4.2 6.8 1.0 C2C A:HEM154 4.3 6.3 1.0 C2A A:HEM154 4.3 5.7 1.0 C3A A:HEM154 4.3 5.7 1.0 CG A:HIS93 4.3 6.8 1.0 C3B A:HEM154 4.3 7.1 1.0 C2B A:HEM154 4.3 6.5 1.0 NE2 A:HIS64 4.6 10.8 1.0 CG2 A:VAL68 4.7 5.0 1.0 CD2 A:HIS97 5.0 9.1 1.0

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