Iron in PDB 1abs: Photolysed Carbonmonoxy-Myoglobin at 20 K

The structure of Photolysed Carbonmonoxy-Myoglobin at 20 K, PDB code: 1abs was solved by I.Schlichting, J.Berendzen, G.N.Phillips Jr., R.M.Sweet, 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 (°)	90.420, 90.420, 45.400, 90.00, 90.00, 120.00
R / Rfree (%)	20.7 / n/a

The binding sites of Iron atom in the Photolysed Carbonmonoxy-Myoglobin at 20 K (pdb code 1abs). 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 Photolysed Carbonmonoxy-Myoglobin at 20 K, PDB code: 1abs:

Iron binding site 1 out of 1 in the Photolysed Carbonmonoxy-Myoglobin at 20 K


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Photolysed Carbonmonoxy-Myoglobin at 20 K within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe154 b:4.6 occ:1.00 FE A:HEM154 0.0 4.6 1.0 NA A:HEM154 2.0 5.0 1.0 ND A:HEM154 2.0 5.0 1.0 NB A:HEM154 2.0 4.9 1.0 NC A:HEM154 2.0 5.5 1.0 NE2 A:HIS93 2.2 5.0 1.0 C4A A:HEM154 3.0 4.9 1.0 C4B A:HEM154 3.0 4.4 1.0 C1B A:HEM154 3.0 4.5 1.0 C1A A:HEM154 3.0 4.9 1.0 C4D A:HEM154 3.0 4.8 1.0 C1D A:HEM154 3.0 5.7 1.0 C1C A:HEM154 3.0 4.2 1.0 C4C A:HEM154 3.0 5.0 1.0 CE1 A:HIS93 3.0 5.8 1.0 CD2 A:HIS93 3.3 5.5 1.0 CHB A:HEM154 3.3 4.7 1.0 CHC A:HEM154 3.4 4.8 1.0 CHA A:HEM154 3.4 4.8 1.0 CHD A:HEM154 3.4 5.3 1.0 O A:CMO155 3.6 7.0 0.9 C A:CMO155 4.1 5.9 1.0 C3A A:HEM154 4.2 5.0 1.0 C3B A:HEM154 4.2 4.3 1.0 C2A A:HEM154 4.2 5.2 1.0 C2B A:HEM154 4.2 4.5 1.0 C3D A:HEM154 4.2 5.8 1.0 C3C A:HEM154 4.2 5.6 1.0 C2D A:HEM154 4.2 5.5 1.0 C2C A:HEM154 4.2 4.8 1.0 ND1 A:HIS93 4.2 5.4 1.0 CG A:HIS93 4.4 5.5 1.0 CG2 A:VAL68 4.6 3.0 1.0 NE2 A:HIS64 4.7 9.7 1.0

I.Schlichting, J.Berendzen, G.N.Phillips Jr., R.M.Sweet. Crystal Structure of Photolysed Carbonmonoxy-Myoglobin. Nature V. 371 808 1994.
ISSN: ISSN 0028-0836
PubMed: 7935843
DOI: 10.1038/371808A0