Iron in PDB 1a6m: Oxy-Myoglobin, Atomic Resolution

The structure of Oxy-Myoglobin, Atomic Resolution, PDB code: 1a6m was solved by J.Vojtechovsky, K.Chu, J.Berendzen, R.M.Sweet, I.Schlichting, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 1.00
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	63.800, 30.810, 34.350, 90.00, 105.80, 90.00
R / Rfree (%)	12.2 / 15.9

The binding sites of Iron atom in the Oxy-Myoglobin, Atomic Resolution (pdb code 1a6m). 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 Oxy-Myoglobin, Atomic Resolution, PDB code: 1a6m:

Iron binding site 1 out of 1 in the Oxy-Myoglobin, Atomic Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Oxy-Myoglobin, Atomic Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe154 b:6.9 occ:1.00 FE A:HEM154 0.0 6.9 1.0 O1 A:OXY157 1.8 8.7 1.0 NB A:HEM154 2.0 6.8 1.0 NA A:HEM154 2.0 7.4 1.0 NC A:HEM154 2.0 7.0 1.0 ND A:HEM154 2.0 7.4 1.0 NE2 A:HIS93 2.1 7.3 1.0 O2 A:OXY157 2.7 13.8 1.0 CE1 A:HIS93 3.0 9.1 1.0 C4C A:HEM154 3.0 6.9 1.0 C1A A:HEM154 3.0 7.9 1.0 C4B A:HEM154 3.0 6.7 1.0 C1B A:HEM154 3.0 7.0 1.0 C1D A:HEM154 3.0 7.7 1.0 C4D A:HEM154 3.0 8.0 1.0 C1C A:HEM154 3.1 7.0 1.0 C4A A:HEM154 3.1 7.5 1.0 CD2 A:HIS93 3.1 7.3 1.0 CHD A:HEM154 3.4 7.6 1.0 CHA A:HEM154 3.4 7.9 1.0 CHC A:HEM154 3.4 6.9 1.0 CHB A:HEM154 3.4 7.3 1.0 ND1 A:HIS93 4.2 9.0 1.0 C3C A:HEM154 4.2 7.3 1.0 CG A:HIS93 4.3 7.7 1.0 C2D A:HEM154 4.3 8.5 1.0 C3D A:HEM154 4.3 8.7 1.0 C2C A:HEM154 4.3 7.2 1.0 C3A A:HEM154 4.3 8.3 1.0 C3B A:HEM154 4.3 6.9 1.0 C2B A:HEM154 4.3 6.9 1.0 C2A A:HEM154 4.3 8.1 1.0 NE2 A:HIS64 4.6 8.0 0.5 CE1 A:HIS64 4.6 6.2 0.5 NE2 A:HIS64 4.7 6.9 0.5 CG2 A:VAL68 4.7 7.0 1.0 CE1 A:HIS64 4.9 7.2 0.5

J.Vojtechovsky, K.Chu, J.Berendzen, R.M.Sweet, I.Schlichting. Crystal Structures of Myoglobin-Ligand Complexes at Near-Atomic Resolution. Biophys.J. V. 77 2153 1999.
ISSN: ISSN 0006-3495
PubMed: 10512835