Iron in PDB 1dm1: 2.0 A Crystal Structure of the Double Mutant H(E7)V, T(E10) R of Myoglobin From Aplysia Limacina

The structure of 2.0 A Crystal Structure of the Double Mutant H(E7)V, T(E10) R of Myoglobin From Aplysia Limacina, PDB code: 1dm1 was solved by L.Federici, C.Savino, R.Musto, C.Travaglini-Allocatelli, F.Cutruzzola, M.Brunori, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	59.76 / 1.99
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	89.730, 89.730, 92.080, 90.00, 90.00, 120.00
R / Rfree (%)	18.9 / 21.6

The binding sites of Iron atom in the 2.0 A Crystal Structure of the Double Mutant H(E7)V, T(E10) R of Myoglobin From Aplysia Limacina (pdb code 1dm1). 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 2.0 A Crystal Structure of the Double Mutant H(E7)V, T(E10) R of Myoglobin From Aplysia Limacina, PDB code: 1dm1:

Iron binding site 1 out of 1 in the 2.0 A Crystal Structure of the Double Mutant H(E7)V, T(E10) R of Myoglobin From Aplysia Limacina


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of 2.0 A Crystal Structure of the Double Mutant H(E7)V, T(E10) R of Myoglobin From Aplysia Limacina within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe148 b:27.1 occ:1.00 FE A:HEM148 0.0 27.1 1.0 NA A:HEM148 1.9 25.1 1.0 NC A:HEM148 2.0 24.7 1.0 ND A:HEM148 2.0 27.0 1.0 NB A:HEM148 2.1 22.6 1.0 NE2 A:HIS95 2.1 23.3 1.0 O A:HOH172 2.2 33.1 1.0 C1A A:HEM148 3.0 28.6 1.0 C4A A:HEM148 3.0 26.4 1.0 C4C A:HEM148 3.0 26.6 1.0 C1C A:HEM148 3.0 27.2 1.0 CE1 A:HIS95 3.0 24.8 1.0 C4D A:HEM148 3.0 25.2 1.0 C1D A:HEM148 3.1 26.5 1.0 C1B A:HEM148 3.1 21.7 1.0 C4B A:HEM148 3.1 22.4 1.0 CD2 A:HIS95 3.2 24.0 1.0 CHA A:HEM148 3.4 26.1 1.0 CHB A:HEM148 3.4 21.8 1.0 CHD A:HEM148 3.4 25.1 1.0 CHC A:HEM148 3.4 24.2 1.0 C2A A:HEM148 4.2 28.1 1.0 C3A A:HEM148 4.2 27.0 1.0 ND1 A:HIS95 4.2 24.2 1.0 C3C A:HEM148 4.2 26.3 1.0 C2C A:HEM148 4.2 26.7 1.0 C3D A:HEM148 4.3 26.9 1.0 C3B A:HEM148 4.3 24.2 1.0 C2D A:HEM148 4.3 28.0 1.0 CG A:HIS95 4.3 24.7 1.0 C2B A:HEM148 4.3 21.5 1.0 O A:HOH199 4.3 49.4 1.0 CG1 A:ILE67 4.7 27.1 1.0

L.Federici, C.Savino, R.Musto, C.Travaglini-Allocatelli, F.Cutruzzola, M.Brunori. Engineering His(E7) Affects the Control of Heme Reactivity in Aplysia Limacina Myoglobin. Biochem.Biophys.Res.Commun. V. 269 58 2000.
ISSN: ISSN 0006-291X
PubMed: 10694477
DOI: 10.1006/BBRC.2000.2259