Iron in PDB 5d5r: Horse-Heart Myoglobin - Deoxy State

The structure of Horse-Heart Myoglobin - Deoxy State, PDB code: 5d5r was solved by T.Barends, I.Schlichting, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	34.21 / 1.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	63.600, 28.800, 35.600, 90.00, 106.50, 90.00
R / Rfree (%)	17.2 / 20.5

The binding sites of Iron atom in the Horse-Heart Myoglobin - Deoxy State (pdb code 5d5r). 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 Horse-Heart Myoglobin - Deoxy State, PDB code: 5d5r:

Iron binding site 1 out of 1 in the Horse-Heart Myoglobin - Deoxy State


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Horse-Heart Myoglobin - Deoxy State within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:12.2 occ:1.00 FE A:HEM201 0.0 12.2 1.0 NB A:HEM201 2.0 11.3 1.0 ND A:HEM201 2.1 13.5 1.0 NA A:HEM201 2.1 11.6 1.0 NC A:HEM201 2.1 11.5 1.0 NE2 A:HIS93 2.2 11.4 1.0 C1B A:HEM201 3.0 12.0 1.0 C4B A:HEM201 3.1 12.5 1.0 C4D A:HEM201 3.1 12.9 1.0 C1A A:HEM201 3.1 12.3 1.0 C4A A:HEM201 3.1 12.2 1.0 C4C A:HEM201 3.1 12.7 1.0 C1D A:HEM201 3.1 12.5 1.0 C1C A:HEM201 3.1 12.1 1.0 CE1 A:HIS93 3.2 12.0 1.0 CD2 A:HIS93 3.2 9.9 1.0 CHB A:HEM201 3.4 12.3 1.0 CHD A:HEM201 3.4 14.4 1.0 CHA A:HEM201 3.4 12.6 1.0 CHC A:HEM201 3.5 12.7 1.0 O A:HOH408 3.7 27.9 1.0 C2B A:HEM201 4.3 11.8 1.0 C3B A:HEM201 4.3 11.2 1.0 ND1 A:HIS93 4.3 13.6 1.0 C3A A:HEM201 4.3 12.5 1.0 C3C A:HEM201 4.3 11.5 1.0 C2A A:HEM201 4.3 11.1 1.0 C2C A:HEM201 4.3 12.2 1.0 C3D A:HEM201 4.3 14.6 1.0 C2D A:HEM201 4.3 13.5 1.0 CG A:HIS93 4.4 14.4 1.0 NE2 A:HIS64 4.5 17.3 1.0 CG2 A:VAL68 4.6 14.1 1.0 CD2 A:HIS97 5.0 15.8 1.0 CE1 A:HIS64 5.0 18.0 1.0

T.R.Barends, L.Foucar, A.Ardevol, K.Nass, A.Aquila, S.Botha, R.B.Doak, K.Falahati, E.Hartmann, M.Hilpert, M.Heinz, M.C.Hoffmann, J.Kofinger, J.E.Koglin, G.Kovacsova, M.Liang, D.Milathianaki, H.T.Lemke, J.Reinstein, C.M.Roome, R.L.Shoeman, G.J.Williams, I.Burghardt, G.Hummer, S.Boutet, I.Schlichting. Direct Observation of Ultrafast Collective Motions in Co Myoglobin Upon Ligand Dissociation. Science V. 350 445 2015.
ISSN: ESSN 1095-9203
PubMed: 26359336
DOI: 10.1126/SCIENCE.AAC5492