Iron in PDB 1irw: Cytochrome C Isozyme 1, Reduced, Mutant with Asn 52 Replaced By Ala and Cys 102 Replaced By Thr

The structure of Cytochrome C Isozyme 1, Reduced, Mutant with Asn 52 Replaced By Ala and Cys 102 Replaced By Thr, PDB code: 1irw 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)	6.00 / 2.00
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	36.520, 36.520, 137.390, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The binding sites of Iron atom in the Cytochrome C Isozyme 1, Reduced, Mutant with Asn 52 Replaced By Ala and Cys 102 Replaced By Thr (pdb code 1irw). 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 Cytochrome C Isozyme 1, Reduced, Mutant with Asn 52 Replaced By Ala and Cys 102 Replaced By Thr, PDB code: 1irw:

Iron binding site 1 out of 1 in the Cytochrome C Isozyme 1, Reduced, Mutant with Asn 52 Replaced By Ala and Cys 102 Replaced By Thr


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Cytochrome C Isozyme 1, Reduced, Mutant with Asn 52 Replaced By Ala and Cys 102 Replaced By Thr within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe104 b:8.8 occ:1.00 FE A:HEM104 0.0 8.8 1.0 NA A:HEM104 2.0 10.3 1.0 NE2 A:HIS18 2.0 4.0 1.0 NC A:HEM104 2.0 8.4 1.0 NB A:HEM104 2.0 6.8 1.0 ND A:HEM104 2.1 10.7 1.0 SD A:MET80 2.3 10.2 1.0 CE1 A:HIS18 2.9 5.0 1.0 C4A A:HEM104 3.0 10.2 1.0 C1B A:HEM104 3.0 10.4 1.0 C4B A:HEM104 3.0 7.9 1.0 CD2 A:HIS18 3.0 4.0 1.0 C1A A:HEM104 3.0 11.0 1.0 C4C A:HEM104 3.0 9.4 1.0 C1C A:HEM104 3.0 8.8 1.0 C4D A:HEM104 3.1 12.3 1.0 C1D A:HEM104 3.1 11.8 1.0 CHC A:HEM104 3.4 8.6 1.0 CHD A:HEM104 3.4 11.6 1.0 CHA A:HEM104 3.4 11.2 1.0 CHB A:HEM104 3.4 9.4 1.0 CG A:MET80 3.5 9.1 1.0 CE A:MET80 3.6 8.2 1.0 ND1 A:HIS18 4.1 4.0 1.0 CG A:HIS18 4.2 4.0 1.0 C2A A:HEM104 4.2 10.2 1.0 C3A A:HEM104 4.2 10.3 1.0 C2C A:HEM104 4.2 9.3 1.0 C2B A:HEM104 4.3 10.6 1.0 C3C A:HEM104 4.3 8.3 1.0 C3B A:HEM104 4.3 9.7 1.0 C2D A:HEM104 4.3 12.1 1.0 C3D A:HEM104 4.3 12.0 1.0 CB A:MET80 4.4 8.9 1.0 OH A:TYR67 4.9 22.9 1.0

S.P.Rafferty, J.G.Guillemette, A.M.Berghuis, M.Smith, G.D.Brayer, A.G.Mauk. Mechanistic and Structural Contributions of Critical Surface and Internal Residues to Cytochrome C Electron Transfer Reactivity. Biochemistry V. 35 10784 1996.
ISSN: ISSN 0006-2960
PubMed: 8718869
DOI: 10.1021/BI960430V