Iron in PDB 1ycb: Distal Pocket Polarity in Ligand Binding to Myoglobin: Deoxy and Carbonmonoxy Forms of A THREONINE68 (E11) Mutant Investigated By X-Ray Crystallography and Infrared Spectroscopy

The structure of Distal Pocket Polarity in Ligand Binding to Myoglobin: Deoxy and Carbonmonoxy Forms of A THREONINE68 (E11) Mutant Investigated By X-Ray Crystallography and Infrared Spectroscopy, PDB code: 1ycb was solved by A.D.Cameron, S.J.Smerdon, A.J.Wilkinson, J.Habash, J.R.Helliwell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 2.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	124.600, 42.500, 92.000, 90.00, 92.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Iron atom in the Distal Pocket Polarity in Ligand Binding to Myoglobin: Deoxy and Carbonmonoxy Forms of A THREONINE68 (E11) Mutant Investigated By X-Ray Crystallography and Infrared Spectroscopy (pdb code 1ycb). 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 Pocket Polarity in Ligand Binding to Myoglobin: Deoxy and Carbonmonoxy Forms of A THREONINE68 (E11) Mutant Investigated By X-Ray Crystallography and Infrared Spectroscopy, PDB code: 1ycb:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Distal Pocket Polarity in Ligand Binding to Myoglobin: Deoxy and Carbonmonoxy Forms of A THREONINE68 (E11) Mutant Investigated By X-Ray Crystallography and Infrared Spectroscopy


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Distal Pocket Polarity in Ligand Binding to Myoglobin: Deoxy and Carbonmonoxy Forms of A THREONINE68 (E11) Mutant Investigated By X-Ray Crystallography and Infrared Spectroscopy within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe154 b:18.1 occ:1.00 FE A:HEM154 0.0 18.1 1.0 O A:HOH160 1.9 14.4 0.3 ND A:HEM154 2.0 17.3 1.0 NA A:HEM154 2.0 16.8 1.0 NC A:HEM154 2.0 17.8 1.0 NB A:HEM154 2.0 16.6 1.0 NE2 A:HIS93 2.1 15.9 1.0 CE1 A:HIS93 2.7 15.5 1.0 C4D A:HEM154 3.0 18.6 1.0 C1A A:HEM154 3.0 17.6 1.0 C4C A:HEM154 3.0 18.4 1.0 C1D A:HEM154 3.0 17.5 1.0 C4A A:HEM154 3.0 17.2 1.0 C4B A:HEM154 3.1 16.1 1.0 C1C A:HEM154 3.1 18.4 1.0 C1B A:HEM154 3.1 15.8 1.0 CHA A:HEM154 3.3 17.7 1.0 CD2 A:HIS93 3.3 15.2 1.0 CHC A:HEM154 3.5 17.1 1.0 CHD A:HEM154 3.5 17.7 1.0 CHB A:HEM154 3.5 16.2 1.0 O A:HOH175 3.5 18.2 0.7 ND1 A:HIS93 4.0 15.5 1.0 C2A A:HEM154 4.2 17.8 1.0 C3D A:HEM154 4.2 18.7 1.0 C3A A:HEM154 4.3 17.4 1.0 C2D A:HEM154 4.3 17.5 1.0 C3C A:HEM154 4.3 18.2 1.0 C2B A:HEM154 4.3 15.8 1.0 C3B A:HEM154 4.3 15.5 1.0 CG A:HIS93 4.3 16.1 1.0 C2C A:HEM154 4.3 18.0 1.0 NE2 A:HIS64 4.3 12.2 1.0 CE1 A:HIS64 4.7 13.8 1.0 OG1 A:THR68 4.9 10.5 1.0

Iron binding site 2 out of 2 in the Distal Pocket Polarity in Ligand Binding to Myoglobin: Deoxy and Carbonmonoxy Forms of A THREONINE68 (E11) Mutant Investigated By X-Ray Crystallography and Infrared Spectroscopy


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Distal Pocket Polarity in Ligand Binding to Myoglobin: Deoxy and Carbonmonoxy Forms of A THREONINE68 (E11) Mutant Investigated By X-Ray Crystallography and Infrared Spectroscopy within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe154 b:16.3 occ:1.00 FE B:HEM154 0.0 16.3 1.0 NA B:HEM154 2.0 14.4 1.0 ND B:HEM154 2.0 15.9 1.0 NC B:HEM154 2.0 14.2 1.0 NB B:HEM154 2.0 13.7 1.0 NE2 B:HIS93 2.2 14.2 1.0 C4A B:HEM154 3.0 14.7 1.0 O B:HOH191 3.0 24.5 1.0 C4D B:HEM154 3.0 17.5 1.0 CE1 B:HIS93 3.0 15.6 1.0 C1D B:HEM154 3.0 16.1 1.0 C1A B:HEM154 3.0 15.5 1.0 C1C B:HEM154 3.1 13.4 1.0 C4C B:HEM154 3.1 14.3 1.0 C1B B:HEM154 3.1 12.4 1.0 C4B B:HEM154 3.1 12.8 1.0 CD2 B:HIS93 3.3 14.6 1.0 CHA B:HEM154 3.4 16.1 1.0 CHB B:HEM154 3.4 13.7 1.0 CHC B:HEM154 3.4 13.1 1.0 CHD B:HEM154 3.6 15.2 1.0 C3D B:HEM154 4.2 18.3 1.0 C3A B:HEM154 4.2 14.7 1.0 C2A B:HEM154 4.2 15.6 1.0 C2D B:HEM154 4.2 17.2 1.0 ND1 B:HIS93 4.3 15.5 1.0 C2C B:HEM154 4.3 13.3 1.0 C3C B:HEM154 4.3 13.3 1.0 C2B B:HEM154 4.3 11.8 1.0 C3B B:HEM154 4.3 11.7 1.0 NE2 B:HIS64 4.4 10.7 1.0 CG B:HIS93 4.4 16.8 1.0 CE1 B:HIS64 4.8 10.4 1.0

A.D.Cameron, S.J.Smerdon, A.J.Wilkinson, J.Habash, J.R.Helliwell, T.Li, J.S.Olson. Distal Pocket Polarity in Ligand Binding to Myoglobin: Deoxy and Carbonmonoxy Forms of A THREONINE68(E11) Mutant Investigated By X-Ray Crystallography and Infrared Spectroscopy. Biochemistry V. 32 13061 1993.
ISSN: ISSN 0006-2960
PubMed: 8241160
DOI: 10.1021/BI00211A016