Iron in PDB 1bbh: Atomic Structure of A Cytochrome C' with An Unusual Ligand-Controlled Dimer Dissociation at 1.8 Angstroms Resolution

The structure of Atomic Structure of A Cytochrome C' with An Unusual Ligand-Controlled Dimer Dissociation at 1.8 Angstroms Resolution, PDB code: 1bbh was solved by Z.Ren, D.E.Mcree, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	5.00 / 1.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	49.200, 56.700, 98.800, 90.00, 90.00, 90.00
R / Rfree (%)	18.5 / n/a

The binding sites of Iron atom in the Atomic Structure of A Cytochrome C' with An Unusual Ligand-Controlled Dimer Dissociation at 1.8 Angstroms Resolution (pdb code 1bbh). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Atomic Structure of A Cytochrome C' with An Unusual Ligand-Controlled Dimer Dissociation at 1.8 Angstroms Resolution, PDB code: 1bbh:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Atomic Structure of A Cytochrome C' with An Unusual Ligand-Controlled Dimer Dissociation at 1.8 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Atomic Structure of A Cytochrome C' with An Unusual Ligand-Controlled Dimer Dissociation at 1.8 Angstroms Resolution within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe132 b:16.1 occ:1.00 FE A:HEM132 0.0 16.1 1.0 NE2 A:HIS125 2.0 16.2 1.0 NA A:HEM132 2.0 12.7 1.0 ND A:HEM132 2.1 13.9 1.0 NB A:HEM132 2.1 15.7 1.0 NC A:HEM132 2.1 13.4 1.0 CE1 A:HIS125 3.0 18.1 1.0 CD2 A:HIS125 3.0 15.1 1.0 C4A A:HEM132 3.0 14.1 1.0 C4D A:HEM132 3.0 9.9 1.0 C1B A:HEM132 3.0 17.6 1.0 C1A A:HEM132 3.0 11.4 1.0 C1D A:HEM132 3.1 11.3 1.0 C1C A:HEM132 3.1 13.6 1.0 C4B A:HEM132 3.1 12.4 1.0 C4C A:HEM132 3.1 12.7 1.0 CHB A:HEM132 3.3 14.1 1.0 CHA A:HEM132 3.4 12.0 1.0 CHD A:HEM132 3.4 9.1 1.0 CHC A:HEM132 3.4 10.5 1.0 CD1 A:TYR16 3.5 11.6 1.0 CG A:TYR16 3.8 10.2 1.0 CE1 A:TYR16 3.8 15.9 1.0 ND1 A:HIS125 4.1 21.2 1.0 CG A:HIS125 4.2 19.7 1.0 C3A A:HEM132 4.2 17.0 1.0 C3D A:HEM132 4.2 13.2 1.0 C2A A:HEM132 4.2 13.9 1.0 CD2 A:TYR16 4.2 16.5 1.0 C2B A:HEM132 4.2 19.1 1.0 CZ A:TYR16 4.3 12.8 1.0 C2D A:HEM132 4.3 14.1 1.0 C2C A:HEM132 4.3 13.8 1.0 C3B A:HEM132 4.3 15.8 1.0 C3C A:HEM132 4.3 13.7 1.0 CB A:TYR16 4.4 15.3 1.0 CE2 A:TYR16 4.5 13.1 1.0 NH2 A:ARG129 4.7 23.1 1.0

Iron binding site 2 out of 2 in the Atomic Structure of A Cytochrome C' with An Unusual Ligand-Controlled Dimer Dissociation at 1.8 Angstroms Resolution


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Atomic Structure of A Cytochrome C' with An Unusual Ligand-Controlled Dimer Dissociation at 1.8 Angstroms Resolution within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe132 b:19.6 occ:1.00 FE B:HEM132 0.0 19.6 1.0 NE2 B:HIS125 2.0 27.4 1.0 NB B:HEM132 2.0 14.7 1.0 ND B:HEM132 2.0 16.1 1.0 NA B:HEM132 2.1 18.2 1.0 NC B:HEM132 2.1 17.9 1.0 CE1 B:HIS125 3.0 27.4 1.0 C4A B:HEM132 3.0 14.1 1.0 C1B B:HEM132 3.0 15.8 1.0 C1D B:HEM132 3.0 18.3 1.0 C4D B:HEM132 3.0 17.8 1.0 C4B B:HEM132 3.1 20.9 1.0 C1A B:HEM132 3.1 20.9 1.0 CD2 B:HIS125 3.1 21.6 1.0 C4C B:HEM132 3.1 16.2 1.0 C1C B:HEM132 3.1 17.5 1.0 CHB B:HEM132 3.3 12.5 1.0 CHD B:HEM132 3.4 16.8 1.0 CHA B:HEM132 3.4 20.5 1.0 CHC B:HEM132 3.4 20.7 1.0 CD1 B:TYR16 3.5 17.0 1.0 CG B:TYR16 3.8 19.7 1.0 CE1 B:TYR16 3.8 14.4 1.0 ND1 B:HIS125 4.1 27.3 1.0 CZ B:TYR16 4.2 18.1 1.0 CG B:HIS125 4.2 24.4 1.0 CD2 B:TYR16 4.2 20.5 1.0 C2D B:HEM132 4.2 20.2 1.0 C3A B:HEM132 4.2 15.9 1.0 C3D B:HEM132 4.2 20.4 1.0 C2B B:HEM132 4.2 18.4 1.0 C3B B:HEM132 4.3 22.5 1.0 C2A B:HEM132 4.3 18.6 1.0 C3C B:HEM132 4.3 18.9 1.0 C2C B:HEM132 4.3 19.1 1.0 CB B:TYR16 4.3 16.2 1.0 CE2 B:TYR16 4.4 15.6 1.0 NH1 B:ARG129 4.5 40.3 1.0 OH B:TYR16 5.0 18.0 1.0

Z.Ren, T.Meyer, D.E.Mcree. Atomic Structure of A Cytochrome C' with An Unusual Ligand-Controlled Dimer Dissociation at 1.8 A Resolution. J.Mol.Biol. V. 234 433 1993.
ISSN: ISSN 0022-2836
PubMed: 8230224
DOI: 10.1006/JMBI.1993.1597