Iron in PDB 256b: Improvement of the 2.5 Angstroms Resolution Model of Cytochrome B562 By Redetermining the Primary Structure and Using Molecular Graphics

The structure of Improvement of the 2.5 Angstroms Resolution Model of Cytochrome B562 By Redetermining the Primary Structure and Using Molecular Graphics, PDB code: 256b was solved by K.Hamada, P.H.Bethge, F.S.Mathews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	6.00 / 1.40
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	33.710, 50.480, 32.730, 102.76, 86.55, 106.70
R / Rfree (%)	n/a / n/a

The binding sites of Iron atom in the Improvement of the 2.5 Angstroms Resolution Model of Cytochrome B562 By Redetermining the Primary Structure and Using Molecular Graphics (pdb code 256b). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Improvement of the 2.5 Angstroms Resolution Model of Cytochrome B562 By Redetermining the Primary Structure and Using Molecular Graphics, PDB code: 256b:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Improvement of the 2.5 Angstroms Resolution Model of Cytochrome B562 By Redetermining the Primary Structure and Using Molecular Graphics


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Improvement of the 2.5 Angstroms Resolution Model of Cytochrome B562 By Redetermining the Primary Structure and Using Molecular Graphics within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe109 b:10.4 occ:1.00 FE A:HEM109 0.0 10.4 1.0 NB A:HEM109 2.0 9.6 1.0 NA A:HEM109 2.0 10.8 1.0 ND A:HEM109 2.0 10.3 1.0 NC A:HEM109 2.0 10.1 1.0 NE2 A:HIS102 2.1 9.0 1.0 SD A:MET7 2.3 10.0 1.0 CE1 A:HIS102 2.9 8.9 1.0 C4B A:HEM109 3.0 9.5 1.0 C1C A:HEM109 3.0 10.1 1.0 C1B A:HEM109 3.0 9.1 1.0 C4D A:HEM109 3.0 11.6 1.0 C4A A:HEM109 3.1 11.5 1.0 C1D A:HEM109 3.1 10.7 1.0 C1A A:HEM109 3.1 12.1 1.0 C4C A:HEM109 3.1 9.6 1.0 CD2 A:HIS102 3.1 9.4 1.0 CE A:MET7 3.3 11.3 1.0 CHA A:HEM109 3.4 12.1 1.0 CHB A:HEM109 3.4 10.1 1.0 CHC A:HEM109 3.4 10.4 1.0 CHD A:HEM109 3.4 10.2 1.0 CG A:MET7 3.5 10.8 1.0 ND1 A:HIS102 4.1 10.4 1.0 CG A:HIS102 4.2 9.5 1.0 CB A:MET7 4.2 9.9 1.0 C2B A:HEM109 4.2 9.2 1.0 C3B A:HEM109 4.3 9.9 1.0 C2D A:HEM109 4.3 11.9 1.0 C3A A:HEM109 4.3 12.7 1.0 C3D A:HEM109 4.3 12.4 1.0 C3C A:HEM109 4.3 10.5 1.0 C2C A:HEM109 4.3 10.4 1.0 C2A A:HEM109 4.3 13.7 1.0

Iron binding site 2 out of 2 in the Improvement of the 2.5 Angstroms Resolution Model of Cytochrome B562 By Redetermining the Primary Structure and Using Molecular Graphics


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Improvement of the 2.5 Angstroms Resolution Model of Cytochrome B562 By Redetermining the Primary Structure and Using Molecular Graphics within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe109 b:10.7 occ:1.00 FE B:HEM109 0.0 10.7 1.0 NE2 B:HIS102 2.0 9.4 1.0 NA B:HEM109 2.0 12.6 1.0 NC B:HEM109 2.0 11.1 1.0 ND B:HEM109 2.0 11.8 1.0 NB B:HEM109 2.0 11.1 1.0 SD B:MET7 2.4 10.3 1.0 CE1 B:HIS102 2.9 8.9 1.0 CD2 B:HIS102 3.0 9.3 1.0 C4D B:HEM109 3.0 13.2 1.0 C1A B:HEM109 3.0 13.0 1.0 C4B B:HEM109 3.0 11.5 1.0 C4A B:HEM109 3.0 12.5 1.0 C1C B:HEM109 3.0 11.4 1.0 C1B B:HEM109 3.1 11.5 1.0 C1D B:HEM109 3.1 12.7 1.0 C4C B:HEM109 3.1 11.2 1.0 CHD B:HEM109 3.4 11.3 1.0 CHA B:HEM109 3.4 12.9 1.0 CHB B:HEM109 3.4 11.6 1.0 CHC B:HEM109 3.4 11.1 1.0 CE B:MET7 3.5 12.2 1.0 CG B:MET7 3.5 10.4 1.0 ND1 B:HIS102 4.0 9.4 1.0 CG B:HIS102 4.1 9.4 1.0 C3A B:HEM109 4.3 13.8 1.0 C3D B:HEM109 4.3 14.3 1.0 C2A B:HEM109 4.3 14.9 1.0 C3C B:HEM109 4.3 11.9 1.0 C2B B:HEM109 4.3 11.1 1.0 C2D B:HEM109 4.3 13.6 1.0 CB B:MET7 4.3 10.0 1.0 C2C B:HEM109 4.3 11.7 1.0 C3B B:HEM109 4.3 12.0 1.0

F.Lederer, A.Glatigny, P.H.Bethge, H.D.Bellamy, F.S.Matthew. Improvement of the 2.5 A Resolution Model of Cytochrome B562 By Redetermining the Primary Structure and Using Molecular Graphics. J.Mol.Biol. V. 148 427 1981.
ISSN: ISSN 0022-2836
PubMed: 7031264
DOI: 10.1016/0022-2836(81)90185-6