Iron in PDB 4cvp: Structure of Apobacterioferritin

All present enzymatic activity of Structure of Apobacterioferritin:
1.16.3.1;

The structure of Structure of Apobacterioferritin, PDB code: 4cvp was solved by K.Hingorani, R.Pace, S.Whitney, J.W.Murray, T.Wydrzynski, M.H.Cheah, P.Smith, W.Hillier, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.64 / 2.11
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	95.970, 28.300, 54.470, 90.00, 103.48, 90.00
R / Rfree (%)	21.573 / 29.877

The binding sites of Iron atom in the Structure of Apobacterioferritin (pdb code 4cvp). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 2 binding sites of Iron where determined in the Structure of Apobacterioferritin, PDB code: 4cvp:
Jump to Iron binding site number: 1; 2;

Iron binding site 1 out of 2 in the Structure of Apobacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Structure of Apobacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1155 b:66.0 occ:1.00 OE1 A:GLU51 2.1 38.9 1.0 OE2 A:GLU127 2.2 33.0 1.0 OE1 A:GLU18 2.3 36.1 1.0 OE2 A:GLU18 2.3 41.5 1.0 ND1 A:HIS54 2.4 26.6 1.0 CD A:GLU18 2.6 34.5 1.0 O A:HOH2006 2.8 31.7 1.0 CD A:GLU127 3.1 29.9 1.0 CD A:GLU51 3.2 34.9 1.0 CE1 A:HIS54 3.2 26.1 1.0 OE1 A:GLU127 3.2 32.2 1.0 CG A:HIS54 3.4 26.4 1.0 OE2 A:GLU51 3.7 36.1 1.0 CB A:HIS54 3.8 24.9 1.0 O A:HOH2007 3.9 32.4 1.0 CG A:GLU18 4.1 33.8 1.0 O A:HOH2008 4.2 22.8 1.0 CA A:GLU51 4.3 34.2 1.0 FE A:FE1156 4.3 73.1 1.0 CG A:GLU51 4.3 34.2 1.0 CB A:GLU51 4.3 33.3 1.0 CG2 A:ILE123 4.3 24.1 1.0 NE2 A:HIS54 4.4 25.9 1.0 CG A:GLU127 4.5 29.7 1.0 CD2 A:HIS54 4.5 26.0 1.0 CB A:GLU18 4.9 29.4 1.0 O A:GLU51 5.0 33.6 1.0

Iron binding site 2 out of 2 in the Structure of Apobacterioferritin


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Structure of Apobacterioferritin within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1156 b:73.1 occ:1.00 OE2 A:GLU51 2.0 36.1 1.0 OE1 A:GLU127 2.4 32.2 1.0 OE2 A:GLU94 2.5 38.1 1.0 OE1 A:GLU94 2.8 37.7 1.0 CD A:GLU94 2.9 33.2 1.0 CD A:GLU51 3.0 34.9 1.0 OE1 A:GLU51 3.2 38.9 1.0 OE2 A:GLU47 3.2 44.0 1.0 CD A:GLU127 3.6 29.9 1.0 O A:HOH2006 3.9 31.7 1.0 CD2 A:HIS130 4.2 35.8 1.0 CD A:GLU47 4.2 40.0 1.0 CB A:HIS130 4.2 30.7 1.0 OE2 A:GLU127 4.3 33.0 1.0 CG A:GLU51 4.3 34.2 1.0 FE A:FE1155 4.3 66.0 1.0 CA A:GLU127 4.3 29.0 1.0 CG A:GLU47 4.4 38.2 1.0 CG A:GLU94 4.4 30.6 1.0 OH A:TYR25 4.4 34.1 1.0 CE2 A:TYR25 4.5 32.9 1.0 CG A:HIS130 4.5 34.4 1.0 O A:HOH2032 4.6 25.8 1.0 CB A:GLU127 4.7 28.9 1.0 CG A:GLU127 4.8 29.7 1.0 O A:GLU127 4.9 27.1 1.0 CZ A:TYR25 5.0 33.2 1.0 N A:GLU127 5.0 29.2 1.0

K.Hingorani, R.Pace, S.Whitney, J.W.Murray, P.Smith, M.H.Cheah, T.Wydrzynski, W.Hillier. Photo-Oxidation of Tyrosine in A Bio-Engineered Bacterioferritin 'Reaction Centre'-A Protein Model For Artificial Photosynthesis. Biochim.Biophys.Acta V.1837 1821 2014.
ISSN: ISSN 0006-3002
PubMed: 25107631
DOI: 10.1016/J.BBABIO.2014.07.019