Iron in PDB 4mu5: Crystal Structure of Murine Neuroglobin Mutant M144W

The structure of Crystal Structure of Murine Neuroglobin Mutant M144W, PDB code: 4mu5 was solved by B.Vallone, G.Avella, C.Savino, C.Ardiccioni, M.Brunori, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.89 / 1.80
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	87.636, 87.636, 115.217, 90.00, 90.00, 120.00
R / Rfree (%)	19.9 / 24.9

The binding sites of Iron atom in the Crystal Structure of Murine Neuroglobin Mutant M144W (pdb code 4mu5). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Crystal Structure of Murine Neuroglobin Mutant M144W, PDB code: 4mu5:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Crystal Structure of Murine Neuroglobin Mutant M144W


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Murine Neuroglobin Mutant M144W within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:24.1 occ:0.73 FE A:HEM201 0.0 24.1 0.7 FE A:HEM201 0.6 16.1 0.3 ND A:HEM201 1.9 21.1 0.3 NC A:HEM201 1.9 21.0 0.7 NA A:HEM201 1.9 21.9 0.7 NA A:HEM201 2.0 22.9 0.3 NE2 A:HIS64 2.0 21.0 0.5 ND A:HEM201 2.1 21.2 0.7 NB A:HEM201 2.1 20.9 0.7 NC A:HEM201 2.1 21.2 0.3 NB A:HEM201 2.2 25.2 0.3 NE2 A:HIS96 2.3 25.8 0.9 NE2 A:HIS64 2.3 26.2 0.5 CE1 A:HIS64 2.8 20.8 0.5 C4D A:HEM201 2.9 24.6 0.3 C1A A:HEM201 2.9 27.4 0.3 C1D A:HEM201 2.9 23.6 0.3 C4C A:HEM201 3.0 25.8 0.7 C4A A:HEM201 3.0 22.6 0.7 C1A A:HEM201 3.0 24.1 0.7 C1D A:HEM201 3.0 28.1 0.7 C1C A:HEM201 3.0 28.4 0.7 C4B A:HEM201 3.0 21.5 0.7 CD2 A:HIS64 3.0 21.4 0.5 NE2 A:HIS96 3.1 28.0 0.1 C4A A:HEM201 3.1 27.0 0.3 C4C A:HEM201 3.1 25.0 0.3 C4D A:HEM201 3.1 28.6 0.7 CD2 A:HIS64 3.1 19.1 0.5 C1B A:HEM201 3.1 24.4 0.7 C1B A:HEM201 3.2 25.2 0.3 C1C A:HEM201 3.2 22.5 0.3 CE1 A:HIS96 3.2 29.7 0.9 CHA A:HEM201 3.3 25.4 0.3 C4B A:HEM201 3.3 26.7 0.3 CD2 A:HIS96 3.3 25.6 0.9 CHD A:HEM201 3.3 27.9 0.7 CHD A:HEM201 3.3 22.1 0.3 CHC A:HEM201 3.4 22.6 0.7 CD2 A:HIS96 3.4 26.8 0.1 CHB A:HEM201 3.5 22.3 0.7 CHA A:HEM201 3.5 25.4 0.7 CE1 A:HIS64 3.5 20.8 0.5 CHB A:HEM201 3.5 27.6 0.3 CHC A:HEM201 3.6 23.8 0.3 ND1 A:HIS64 4.0 19.4 0.5 C3D A:HEM201 4.1 27.9 0.3 C2D A:HEM201 4.1 21.9 0.3 CG A:HIS64 4.2 21.9 0.5 C2A A:HEM201 4.2 23.5 0.3 C3C A:HEM201 4.2 26.0 0.7 C3A A:HEM201 4.2 27.1 0.3 CE1 A:HIS96 4.2 27.8 0.1 C3A A:HEM201 4.3 22.0 0.7 C2A A:HEM201 4.3 28.9 0.7 CG A:HIS64 4.3 21.8 0.5 C2C A:HEM201 4.3 30.0 0.7 C3C A:HEM201 4.3 23.6 0.3 C3B A:HEM201 4.4 24.7 0.7 C2D A:HEM201 4.4 26.7 0.7 ND1 A:HIS96 4.4 20.6 0.9 C3D A:HEM201 4.4 24.4 0.7 C2C A:HEM201 4.4 25.1 0.3 C2B A:HEM201 4.4 23.4 0.7 C2B A:HEM201 4.4 26.0 0.3 CG A:HIS96 4.4 31.9 0.9 ND1 A:HIS64 4.5 20.8 0.5 C3B A:HEM201 4.5 29.5 0.3 CG A:HIS96 4.7 29.2 0.1 CG2 A:VAL68 4.8 22.6 1.0

Iron binding site 2 out of 2 in the Crystal Structure of Murine Neuroglobin Mutant M144W


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Murine Neuroglobin Mutant M144W within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe201 b:16.1 occ:0.27 FE A:HEM201 0.0 16.1 0.3 FE A:HEM201 0.6 24.1 0.7 NC A:HEM201 1.7 21.0 0.7 NE2 A:HIS96 1.8 25.8 0.9 NC A:HEM201 1.9 21.2 0.3 NB A:HEM201 1.9 20.9 0.7 NB A:HEM201 2.0 25.2 0.3 ND A:HEM201 2.1 21.1 0.3 NA A:HEM201 2.2 21.9 0.7 NA A:HEM201 2.2 22.9 0.3 ND A:HEM201 2.3 21.2 0.7 NE2 A:HIS64 2.5 21.0 0.5 NE2 A:HIS96 2.6 28.0 0.1 C1C A:HEM201 2.7 28.4 0.7 C4B A:HEM201 2.8 21.5 0.7 CE1 A:HIS96 2.8 29.7 0.9 NE2 A:HIS64 2.8 26.2 0.5 CD2 A:HIS96 2.8 25.6 0.9 C4C A:HEM201 2.8 25.8 0.7 CD2 A:HIS96 2.9 26.8 0.1 C1C A:HEM201 2.9 22.5 0.3 C4B A:HEM201 3.0 26.7 0.3 C4C A:HEM201 3.0 25.0 0.3 C1B A:HEM201 3.1 25.2 0.3 C1B A:HEM201 3.1 24.4 0.7 CHC A:HEM201 3.1 22.6 0.7 C1D A:HEM201 3.1 23.6 0.3 C1D A:HEM201 3.2 28.1 0.7 C4D A:HEM201 3.2 24.6 0.3 C4A A:HEM201 3.2 27.0 0.3 C1A A:HEM201 3.2 27.4 0.3 C4A A:HEM201 3.2 22.6 0.7 CE1 A:HIS64 3.2 20.8 0.5 CHC A:HEM201 3.3 23.8 0.3 C1A A:HEM201 3.3 24.1 0.7 CHD A:HEM201 3.4 27.9 0.7 C4D A:HEM201 3.4 28.6 0.7 CHD A:HEM201 3.4 22.1 0.3 CHB A:HEM201 3.5 27.6 0.3 CHB A:HEM201 3.5 22.3 0.7 CHA A:HEM201 3.5 25.4 0.3 CD2 A:HIS64 3.6 21.4 0.5 CD2 A:HIS64 3.7 19.1 0.5 CHA A:HEM201 3.8 25.4 0.7 CE1 A:HIS96 3.8 27.8 0.1 CE1 A:HIS64 3.9 20.8 0.5 ND1 A:HIS96 3.9 20.6 0.9 CG A:HIS96 4.0 31.9 0.9 C2C A:HEM201 4.0 30.0 0.7 C3C A:HEM201 4.0 26.0 0.7 C3B A:HEM201 4.1 24.7 0.7 C2C A:HEM201 4.2 25.1 0.3 CG A:HIS96 4.2 29.2 0.1 C3C A:HEM201 4.2 23.6 0.3 C3B A:HEM201 4.2 29.5 0.3 C2B A:HEM201 4.2 26.0 0.3 C2B A:HEM201 4.3 23.4 0.7 C2D A:HEM201 4.4 21.9 0.3 C3A A:HEM201 4.4 27.1 0.3 C3D A:HEM201 4.4 27.9 0.3 C2A A:HEM201 4.4 23.5 0.3 ND1 A:HIS64 4.5 19.4 0.5 C3A A:HEM201 4.5 22.0 0.7 C2D A:HEM201 4.5 26.7 0.7 C2A A:HEM201 4.6 28.9 0.7 ND1 A:HIS96 4.6 30.4 0.1 C3D A:HEM201 4.6 24.4 0.7 CG A:HIS64 4.7 21.9 0.5 CG A:HIS64 4.8 21.8 0.5 ND1 A:HIS64 4.9 20.8 0.5 CG2 A:VAL68 5.0 22.6 1.0

G.Avella, C.Ardiccioni, A.Scaglione, T.Moschetti, C.Rondinelli, L.C.Montemiglio, C.Savino, A.Giuffre, M.Brunori, B.Vallone. Engineering the Internal Cavity of Neuroglobin Demonstrates the Role of the Haem-Sliding Mechanism. Acta Crystallogr.,Sect.D V. 70 1640 2014.
ISSN: ISSN 0907-4449
PubMed: 24914975
DOI: 10.1107/S1399004714007032