Iron in PDB 2g14: Photolyzed Co L29F Myoglobin: 3.16US

The structure of Photolyzed Co L29F Myoglobin: 3.16US, PDB code: 2g14 was solved by R.Aranda, E.J.Levin, F.Schotte, P.A.Anfinrud, G.N.Phillips Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.88 / 1.90
Space group	P 6
Cell size a, b, c (Å), α, β, γ (°)	91.200, 91.200, 45.712, 90.00, 90.00, 120.00
R / Rfree (%)	5.1 / 5.8

The binding sites of Iron atom in the Photolyzed Co L29F Myoglobin: 3.16US (pdb code 2g14). 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 Photolyzed Co L29F Myoglobin: 3.16US, PDB code: 2g14:

Iron binding site 1 out of 1 in the Photolyzed Co L29F Myoglobin: 3.16US


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Photolyzed Co L29F Myoglobin: 3.16US within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe154 b:13.6 occ:0.77 FE A:HEM154 0.0 13.6 0.8 C A:CMO155 1.8 14.8 0.8 NC A:HEM154 2.0 14.4 0.8 ND A:HEM154 2.0 14.5 0.8 NB A:HEM154 2.0 14.3 0.8 NA A:HEM154 2.0 13.7 0.8 NE2 A:HIS93 2.2 13.7 0.8 O A:CMO155 2.9 16.1 0.8 C1C A:HEM154 3.0 14.1 0.8 C4D A:HEM154 3.0 15.0 0.8 C4B A:HEM154 3.0 13.8 0.8 C1D A:HEM154 3.0 16.0 0.8 C4C A:HEM154 3.0 15.0 0.8 C4A A:HEM154 3.0 13.7 0.8 C1A A:HEM154 3.0 14.6 0.8 C1B A:HEM154 3.0 14.3 0.8 CD2 A:HIS93 3.2 15.0 0.8 CE1 A:HIS93 3.2 15.2 0.8 CHC A:HEM154 3.4 14.5 0.8 CHD A:HEM154 3.4 14.8 0.8 CHA A:HEM154 3.4 14.7 0.8 CHB A:HEM154 3.4 13.8 0.8 C3D A:HEM154 4.2 16.5 0.8 C2C A:HEM154 4.3 15.4 0.8 C2D A:HEM154 4.3 16.7 0.8 C3C A:HEM154 4.3 16.9 0.8 C3A A:HEM154 4.3 14.4 0.8 C2A A:HEM154 4.3 15.2 0.8 C3B A:HEM154 4.3 14.2 0.8 C2B A:HEM154 4.3 14.4 0.8 CG A:HIS93 4.3 13.4 0.8 ND1 A:HIS93 4.3 15.3 0.8 CG2 A:VAL68 4.7 13.1 0.8 CE1 A:HIS64 4.9 18.4 0.8

R.Aranda, E.J.Levin, F.Schotte, P.A.Anfinrud, G.N.Phillips Jr.. Time-Dependent Atomic Coordinates For the Dissociation of Carbon Monoxide From Myoglobin. Acta Crystallogr.,Sect.D V. 62 776 2006.
ISSN: ISSN 0907-4449
PubMed: 16790933
DOI: 10.1107/S0907444906017318