Iron in PDB 4uzv: Structure of A Triple Mutant of Asv-Tftrhb

The structure of Structure of A Triple Mutant of Asv-Tftrhb, PDB code: 4uzv was solved by P.Baiocco, A.Bonamore, N.Sciamanna, A.Ilari, L.Boechi, A.Boffi, G.Smulevich, A.Feis, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.00 / 3.40
Space group	P 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	78.367, 78.367, 89.806, 90.00, 90.00, 90.00
R / Rfree (%)	29.959 / 34.904

The binding sites of Iron atom in the Structure of A Triple Mutant of Asv-Tftrhb (pdb code 4uzv). 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 Structure of A Triple Mutant of Asv-Tftrhb, PDB code: 4uzv:

Iron binding site 1 out of 1 in the Structure of A Triple Mutant of Asv-Tftrhb


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of A Triple Mutant of Asv-Tftrhb within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1157 b:85.7 occ:1.00 FE A:HEM1157 0.0 85.7 1.0 NA A:HEM1157 2.0 86.8 1.0 NC A:HEM1157 2.0 85.3 1.0 NB A:HEM1157 2.0 85.4 1.0 ND A:HEM1157 2.1 85.8 1.0 NE2 A:HIS106 2.1 90.0 1.0 OXT A:ACT1160 2.9 90.0 0.8 CE1 A:HIS106 2.9 90.0 1.0 C4A A:HEM1157 3.0 87.3 1.0 C1A A:HEM1157 3.0 88.1 1.0 C1C A:HEM1157 3.0 84.9 1.0 C1B A:HEM1157 3.0 85.8 1.0 C4C A:HEM1157 3.0 85.1 1.0 C4B A:HEM1157 3.1 84.8 1.0 C4D A:HEM1157 3.1 86.6 1.0 C1D A:HEM1157 3.1 85.3 1.0 O A:ACT1160 3.2 90.0 0.8 CD2 A:HIS106 3.3 90.0 1.0 C A:ACT1160 3.3 90.0 0.8 CHB A:HEM1157 3.4 86.6 1.0 CHA A:HEM1157 3.4 87.2 1.0 CHC A:HEM1157 3.4 84.6 1.0 CHD A:HEM1157 3.5 84.8 1.0 ND1 A:HIS106 4.1 90.0 1.0 C3A A:HEM1157 4.2 88.8 1.0 C2A A:HEM1157 4.2 89.8 1.0 C2C A:HEM1157 4.3 84.7 1.0 C3C A:HEM1157 4.3 84.9 1.0 C3B A:HEM1157 4.3 85.2 1.0 C2B A:HEM1157 4.3 85.3 1.0 CG A:HIS106 4.3 90.0 1.0 C3D A:HEM1157 4.3 87.0 1.0 C2D A:HEM1157 4.3 86.1 1.0 CH3 A:ACT1160 4.5 90.0 0.8 CE2 A:PHE119 4.9 87.3 1.0

B.Patrizi, A.Lapini, M.Di Donato, A.Marcelli, M.Lima, R.Righini, P.Foggi, P.Baiocco, A.Bonamore, A.Boffi. Role of Local Structure and Dynamics of Small Ligand Migration in Proteins: A Study of A Mutated Truncated Hemoprotein From Thermobifida Fusca By Time Resolved Mir Spectroscopy. J.Phys.Chem.B V. 118 9209 2014.
ISSN: ISSN 1520-6106
PubMed: 25019316
DOI: 10.1021/JP504499B