Iron in PDB 1cri: The Role of A Conserved Internal Water Molecule and Its Associated Hydrogen Bond Network in Cytochrome C

The structure of The Role of A Conserved Internal Water Molecule and Its Associated Hydrogen Bond Network in Cytochrome C, PDB code: 1cri was solved by A.M.Berghuis, G.D.Brayer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	N/A / 2.00
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	36.520, 36.520, 139.120, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Iron atom in the The Role of A Conserved Internal Water Molecule and Its Associated Hydrogen Bond Network in Cytochrome C (pdb code 1cri). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total only one binding site of Iron was determined in the The Role of A Conserved Internal Water Molecule and Its Associated Hydrogen Bond Network in Cytochrome C, PDB code: 1cri:

Iron binding site 1 out of 1 in the The Role of A Conserved Internal Water Molecule and Its Associated Hydrogen Bond Network in Cytochrome C


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Role of A Conserved Internal Water Molecule and Its Associated Hydrogen Bond Network in Cytochrome C within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe104 b:14.0 occ:1.00 FE A:HEM104 0.0 14.0 1.0 NB A:HEM104 1.9 9.4 1.0 NC A:HEM104 2.0 12.2 1.0 NA A:HEM104 2.0 9.0 1.0 ND A:HEM104 2.0 11.6 1.0 NE2 A:HIS18 2.0 11.5 1.0 SD A:MET80 2.5 12.0 1.0 C4B A:HEM104 3.0 10.2 1.0 C1B A:HEM104 3.0 12.4 1.0 CE1 A:HIS18 3.0 13.4 1.0 C4C A:HEM104 3.0 12.6 1.0 C1C A:HEM104 3.0 12.8 1.0 C4A A:HEM104 3.0 8.3 1.0 CD2 A:HIS18 3.0 14.1 1.0 C1A A:HEM104 3.0 9.3 1.0 C1D A:HEM104 3.1 13.4 1.0 C4D A:HEM104 3.1 12.1 1.0 CE A:MET80 3.4 11.4 1.0 CHC A:HEM104 3.4 11.4 1.0 CHB A:HEM104 3.4 9.9 1.0 CHD A:HEM104 3.4 14.4 1.0 CG A:MET80 3.4 9.8 1.0 CHA A:HEM104 3.5 11.2 1.0 ND1 A:HIS18 4.1 16.0 1.0 CG A:HIS18 4.1 14.3 1.0 C2B A:HEM104 4.2 12.6 1.0 C3B A:HEM104 4.2 11.0 1.0 C2C A:HEM104 4.2 13.3 1.0 C3C A:HEM104 4.2 13.7 1.0 C3A A:HEM104 4.3 8.5 1.0 C2A A:HEM104 4.3 9.2 1.0 C3D A:HEM104 4.3 12.3 1.0 C2D A:HEM104 4.3 11.7 1.0 CB A:MET80 4.4 13.6 1.0

A.M.Berghuis, J.G.Guillemette, G.Mclendon, F.Sherman, M.Smith, G.D.Brayer. The Role of A Conserved Internal Water Molecule and Its Associated Hydrogen Bond Network in Cytochrome C. J.Mol.Biol. V. 236 786 1994.
ISSN: ISSN 0022-2836
PubMed: 8114094