Iron in PDB 1myj: Distal Polarity in Ligand Binding to Myoglobin: Structural and Functional Characterization of A THREONINE68(E11) Mutant

The structure of Distal Polarity in Ligand Binding to Myoglobin: Structural and Functional Characterization of A THREONINE68(E11) Mutant, PDB code: 1myj was solved by S.J.Smerdon, T.J.Oldfield, A.J.Wilkinson, Z.Dauter, K.Petratos, K.S.Wilson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	7.00 / 1.90
Space group	I 21
Cell size a, b, c (Å), α, β, γ (°)	123.750, 42.480, 92.050, 90.00, 92.05, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Iron atom in the Distal Polarity in Ligand Binding to Myoglobin: Structural and Functional Characterization of A THREONINE68(E11) Mutant (pdb code 1myj). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Distal Polarity in Ligand Binding to Myoglobin: Structural and Functional Characterization of A THREONINE68(E11) Mutant, PDB code: 1myj:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Distal Polarity in Ligand Binding to Myoglobin: Structural and Functional Characterization of A THREONINE68(E11) Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Distal Polarity in Ligand Binding to Myoglobin: Structural and Functional Characterization of A THREONINE68(E11) Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe155 b:14.1 occ:1.00 FE A:HEM155 0.0 14.1 1.0 NA A:HEM155 1.9 13.5 1.0 O A:HOH190 2.0 13.4 1.0 NC A:HEM155 2.0 14.8 1.0 ND A:HEM155 2.0 15.6 1.0 NB A:HEM155 2.1 13.6 1.0 NE2 A:HIS93 2.1 16.9 1.0 C1A A:HEM155 3.0 16.5 1.0 C4A A:HEM155 3.0 15.4 1.0 C4D A:HEM155 3.1 18.0 1.0 C4C A:HEM155 3.1 16.4 1.0 C1D A:HEM155 3.1 17.4 1.0 C1C A:HEM155 3.1 15.7 1.0 C4B A:HEM155 3.1 13.8 1.0 C1B A:HEM155 3.1 14.0 1.0 CE1 A:HIS93 3.1 17.9 1.0 CD2 A:HIS93 3.2 16.8 1.0 CHA A:HEM155 3.4 16.9 1.0 CHD A:HEM155 3.4 16.8 1.0 CHC A:HEM155 3.5 14.6 1.0 CHB A:HEM155 3.5 14.3 1.0 C2A A:HEM155 4.2 16.4 1.0 C3A A:HEM155 4.2 15.6 1.0 ND1 A:HIS93 4.2 17.5 1.0 C3D A:HEM155 4.3 19.7 1.0 NE2 A:HIS64 4.3 14.4 1.0 C3C A:HEM155 4.3 16.8 1.0 C2C A:HEM155 4.3 16.4 1.0 C2D A:HEM155 4.3 18.7 1.0 CG A:HIS93 4.3 18.3 1.0 C3B A:HEM155 4.3 13.3 1.0 C2B A:HEM155 4.4 13.3 1.0 OG1 A:THR68 4.7 9.4 1.0 CE1 A:HIS64 4.9 14.6 1.0

Iron binding site 2 out of 2 in the Distal Polarity in Ligand Binding to Myoglobin: Structural and Functional Characterization of A THREONINE68(E11) Mutant


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Distal Polarity in Ligand Binding to Myoglobin: Structural and Functional Characterization of A THREONINE68(E11) Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe155 b:13.1 occ:1.00 FE B:HEM155 0.0 13.1 1.0 NA B:HEM155 1.9 10.5 1.0 NC B:HEM155 2.0 12.6 1.0 ND B:HEM155 2.0 13.0 1.0 NB B:HEM155 2.1 10.3 1.0 O B:HOH187 2.1 11.9 1.0 NE2 B:HIS93 2.1 14.1 1.0 C1A B:HEM155 3.0 14.0 1.0 C1D B:HEM155 3.0 14.0 1.0 C4A B:HEM155 3.0 11.9 1.0 C4C B:HEM155 3.0 13.3 1.0 C4B B:HEM155 3.0 10.6 1.0 C1C B:HEM155 3.1 13.4 1.0 C1B B:HEM155 3.1 9.8 1.0 C4D B:HEM155 3.1 14.4 1.0 CD2 B:HIS93 3.1 17.6 1.0 CE1 B:HIS93 3.1 16.6 1.0 CHC B:HEM155 3.4 11.6 1.0 CHD B:HEM155 3.4 13.4 1.0 CHA B:HEM155 3.5 13.1 1.0 CHB B:HEM155 3.5 10.5 1.0 C3D B:HEM155 4.2 16.6 1.0 C3C B:HEM155 4.2 14.9 1.0 ND1 B:HIS93 4.2 17.8 1.0 C2A B:HEM155 4.2 14.1 1.0 C3A B:HEM155 4.2 12.4 1.0 C2D B:HEM155 4.2 15.6 1.0 NE2 B:HIS64 4.3 11.9 1.0 C2C B:HEM155 4.3 14.4 1.0 CG B:HIS93 4.3 18.1 1.0 C3B B:HEM155 4.3 10.2 1.0 C2B B:HEM155 4.3 10.2 1.0 OG1 B:THR68 4.6 9.4 1.0 CE1 B:HIS64 4.9 10.9 1.0

S.J.Smerdon, G.G.Dodson, A.J.Wilkinson, Q.H.Gibson, R.S.Blackmore, T.E.Carver, J.S.Olson. Distal Pocket Polarity in Ligand Binding to Myoglobin: Structural and Functional Characterization of A THREONINE68(E11) Mutant. Biochemistry V. 30 6252 1991.
ISSN: ISSN 0006-2960
PubMed: 1905570
DOI: 10.1021/BI00239A025