Iron in PDB 1pmb: The Determination of the Crystal Structure of Recombinant Pig Myoglobin By Molecular Replacement and Its Refinement

The structure of The Determination of the Crystal Structure of Recombinant Pig Myoglobin By Molecular Replacement and Its Refinement, PDB code: 1pmb was solved by S.J.Smerdon, T.J.Oldfield, E.J.Dodson, G.G.Dodson, R.E.Hubbard, A.J.Wilkinson, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 2.50
Space group	I 21
Cell size a, b, c (Å), α, β, γ (°)	124.910, 42.630, 92.200, 90.00, 92.16, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Iron atom in the The Determination of the Crystal Structure of Recombinant Pig Myoglobin By Molecular Replacement and Its Refinement (pdb code 1pmb). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the The Determination of the Crystal Structure of Recombinant Pig Myoglobin By Molecular Replacement and Its Refinement, PDB code: 1pmb:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the The Determination of the Crystal Structure of Recombinant Pig Myoglobin By Molecular Replacement and Its Refinement


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Determination of the Crystal Structure of Recombinant Pig Myoglobin By Molecular Replacement and Its Refinement within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe154 b:26.1 occ:1.00 FE A:HEM154 0.0 26.1 1.0 ND A:HEM154 2.0 46.4 1.0 NA A:HEM154 2.0 14.9 1.0 NC A:HEM154 2.0 14.1 1.0 NB A:HEM154 2.1 25.6 1.0 NE2 A:HIS93 2.4 24.2 1.0 O A:HOH156 2.8 27.1 1.0 C4C A:HEM154 3.0 35.8 1.0 C4D A:HEM154 3.0 14.8 1.0 C1A A:HEM154 3.0 25.8 1.0 C1D A:HEM154 3.0 18.3 1.0 C1C A:HEM154 3.1 21.8 1.0 C4A A:HEM154 3.1 17.4 1.0 C4B A:HEM154 3.1 12.4 1.0 C1B A:HEM154 3.1 13.6 1.0 CHA A:HEM154 3.3 25.1 1.0 CD2 A:HIS93 3.4 13.9 1.0 CE1 A:HIS93 3.4 13.7 1.0 CHD A:HEM154 3.4 16.8 1.0 CHC A:HEM154 3.5 24.2 1.0 CHB A:HEM154 3.5 14.8 1.0 NE2 A:HIS64 4.2 22.1 1.0 C3D A:HEM154 4.2 32.1 1.0 C3C A:HEM154 4.3 36.2 1.0 C2D A:HEM154 4.3 45.7 1.0 C2A A:HEM154 4.3 30.7 1.0 C2C A:HEM154 4.3 18.3 1.0 C3A A:HEM154 4.3 13.2 1.0 C3B A:HEM154 4.3 14.2 1.0 CG2 A:VAL68 4.4 13.4 1.0 C2B A:HEM154 4.4 25.1 1.0 ND1 A:HIS93 4.5 22.6 1.0 CG A:HIS93 4.5 24.6 1.0 CE1 A:HIS64 4.7 22.4 1.0 CD2 A:HIS97 4.9 26.4 1.0

Iron binding site 2 out of 2 in the The Determination of the Crystal Structure of Recombinant Pig Myoglobin By Molecular Replacement and Its Refinement


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The Determination of the Crystal Structure of Recombinant Pig Myoglobin By Molecular Replacement and Its Refinement within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe154 b:25.3 occ:1.00 FE B:HEM154 0.0 25.3 1.0 NC B:HEM154 2.0 11.6 1.0 ND B:HEM154 2.0 27.0 1.0 NA B:HEM154 2.0 15.6 1.0 NB B:HEM154 2.0 25.5 1.0 NE2 B:HIS93 2.3 23.0 1.0 O B:HOH159 2.7 29.8 1.0 C1D B:HEM154 3.0 21.9 1.0 C1B B:HEM154 3.0 14.3 1.0 C4A B:HEM154 3.0 15.4 1.0 C4C B:HEM154 3.0 31.0 1.0 C4D B:HEM154 3.1 14.4 1.0 C1C B:HEM154 3.1 25.4 1.0 C4B B:HEM154 3.1 15.7 1.0 C1A B:HEM154 3.1 23.7 1.0 CD2 B:HIS93 3.2 12.4 1.0 CE1 B:HIS93 3.3 11.8 1.0 CHB B:HEM154 3.4 15.0 1.0 CHD B:HEM154 3.5 15.5 1.0 CHC B:HEM154 3.5 21.1 1.0 CHA B:HEM154 3.5 10.7 1.0 C3D B:HEM154 4.2 37.2 1.0 C2D B:HEM154 4.3 35.6 1.0 C2B B:HEM154 4.3 18.3 1.0 C3A B:HEM154 4.3 14.4 1.0 C2A B:HEM154 4.3 24.5 1.0 C2C B:HEM154 4.3 15.7 1.0 C3C B:HEM154 4.3 33.1 1.0 C3B B:HEM154 4.3 15.8 1.0 NE2 B:HIS64 4.3 21.7 1.0 CG B:HIS93 4.3 35.9 1.0 ND1 B:HIS93 4.3 24.6 1.0 CG2 B:VAL68 4.6 13.9 1.0 CE1 B:HIS64 4.7 14.3 1.0

S.J.Smerdon, T.J.Oldfield, E.J.Dodson, G.G.Dodson, R.E.Hubbard, A.J.Wilkinson. Determination of the Crystal Structure of Recombinant Pig Myoglobin By Molecular Replacement and Its Refinement. Acta Crystallogr.,Sect.B V. 46 370 1990.
ISSN: ISSN 0108-7681
PubMed: 2383370
DOI: 10.1107/S0108768189012450