Iron in PDB 1ft6: Reduced State of Cytochrome C554 From Nitrosomonas Europaea

The structure of Reduced State of Cytochrome C554 From Nitrosomonas Europaea, PDB code: 1ft6 was solved by T.M.Iverson, D.M.Arciero, A.B.Hooper, D.C.Rees, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 1.80
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	147.240, 147.240, 33.880, 90.00, 90.00, 120.00
R / Rfree (%)	19.7 / 23.6

The binding sites of Iron atom in the Reduced State of Cytochrome C554 From Nitrosomonas Europaea (pdb code 1ft6). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Reduced State of Cytochrome C554 From Nitrosomonas Europaea, PDB code: 1ft6:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Reduced State of Cytochrome C554 From Nitrosomonas Europaea


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Reduced State of Cytochrome C554 From Nitrosomonas Europaea within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe213 b:26.6 occ:1.00 FE A:HEM213 0.0 26.6 1.0 NA A:HEM213 1.9 28.0 1.0 NC A:HEM213 2.0 29.7 1.0 NE2 A:HIS15 2.0 26.7 1.0 NB A:HEM213 2.0 25.9 1.0 ND A:HEM213 2.0 26.6 1.0 ND1 A:HIS102 2.1 26.3 1.0 CE1 A:HIS15 2.8 31.1 1.0 CE1 A:HIS102 2.9 26.7 1.0 C4A A:HEM213 3.0 29.1 1.0 C1A A:HEM213 3.0 26.5 1.0 C1B A:HEM213 3.0 28.1 1.0 C4C A:HEM213 3.0 30.8 1.0 C4D A:HEM213 3.0 28.2 1.0 C1D A:HEM213 3.1 30.1 1.0 C1C A:HEM213 3.1 30.6 1.0 C4B A:HEM213 3.1 28.2 1.0 CD2 A:HIS15 3.2 28.4 1.0 CG A:HIS102 3.2 25.5 1.0 CHB A:HEM213 3.3 27.8 1.0 CHA A:HEM213 3.4 28.2 1.0 CHD A:HEM213 3.4 32.3 1.0 CHC A:HEM213 3.5 29.1 1.0 CB A:HIS102 3.7 29.3 1.0 ND1 A:HIS15 4.1 28.7 1.0 NE2 A:HIS102 4.1 27.5 1.0 C2A A:HEM213 4.2 27.7 1.0 C3A A:HEM213 4.2 24.8 1.0 CG A:HIS15 4.2 30.7 1.0 C3C A:HEM213 4.3 32.8 1.0 CD2 A:HIS102 4.3 25.6 1.0 C3D A:HEM213 4.3 28.4 1.0 C2B A:HEM213 4.3 25.4 1.0 C2C A:HEM213 4.3 30.9 1.0 C2D A:HEM213 4.3 27.2 1.0 C3B A:HEM213 4.3 26.0 1.0

Iron binding site 2 out of 4 in the Reduced State of Cytochrome C554 From Nitrosomonas Europaea


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Reduced State of Cytochrome C554 From Nitrosomonas Europaea within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe214 b:21.3 occ:1.00 FE A:HEM214 0.0 21.3 1.0 NA A:HEM214 2.0 23.7 1.0 NC A:HEM214 2.0 20.0 1.0 NB A:HEM214 2.0 21.8 1.0 ND A:HEM214 2.1 19.6 1.0 NE2 A:HIS64 2.2 18.9 1.0 C4B A:HEM214 3.1 21.3 1.0 C4C A:HEM214 3.1 20.2 1.0 C1A A:HEM214 3.1 23.5 1.0 C1B A:HEM214 3.1 22.2 1.0 CE1 A:HIS64 3.1 24.1 1.0 C1C A:HEM214 3.1 18.6 1.0 C4D A:HEM214 3.1 21.0 1.0 C1D A:HEM214 3.1 23.8 1.0 C4A A:HEM214 3.1 23.7 1.0 CD2 A:HIS64 3.3 24.0 1.0 CHA A:HEM214 3.5 20.4 1.0 CHC A:HEM214 3.5 20.9 1.0 CHD A:HEM214 3.5 22.2 1.0 CHB A:HEM214 3.5 22.9 1.0 CD1 A:PHE156 4.1 28.5 1.0 CE1 A:PHE156 4.1 28.6 1.0 ND1 A:HIS64 4.3 24.1 1.0 C2B A:HEM214 4.3 22.9 1.0 C3C A:HEM214 4.3 21.0 1.0 C3B A:HEM214 4.3 21.9 1.0 C2A A:HEM214 4.3 25.3 1.0 C2C A:HEM214 4.3 19.4 1.0 C3D A:HEM214 4.3 21.3 1.0 C3A A:HEM214 4.3 25.4 1.0 C2D A:HEM214 4.3 21.6 1.0 CD A:PRO155 4.4 29.3 1.0 CG A:HIS64 4.4 21.8 1.0 CMD A:HEM216 4.5 31.4 1.0 OG1 A:THR154 4.6 24.4 1.0 CD2 A:LEU34 5.0 23.8 1.0

Iron binding site 3 out of 4 in the Reduced State of Cytochrome C554 From Nitrosomonas Europaea


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Reduced State of Cytochrome C554 From Nitrosomonas Europaea within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe215 b:24.9 occ:1.00 FE A:HEM215 0.0 24.9 1.0 ND A:HEM215 1.9 24.1 1.0 NB A:HEM215 2.0 28.0 1.0 NC A:HEM215 2.0 24.5 1.0 NA A:HEM215 2.0 22.4 1.0 NE2 A:HIS92 2.0 22.3 1.0 NE2 A:HIS179 2.1 26.2 1.0 CE1 A:HIS92 3.0 23.0 1.0 C4D A:HEM215 3.0 24.6 1.0 C1D A:HEM215 3.0 24.8 1.0 C1A A:HEM215 3.0 28.3 1.0 C4C A:HEM215 3.0 22.9 1.0 C1C A:HEM215 3.0 23.2 1.0 C4B A:HEM215 3.0 27.4 1.0 C1B A:HEM215 3.1 27.5 1.0 C4A A:HEM215 3.1 26.0 1.0 CE1 A:HIS179 3.1 26.9 1.0 CD2 A:HIS92 3.2 23.2 1.0 CD2 A:HIS179 3.2 26.5 1.0 CHA A:HEM215 3.4 26.4 1.0 CHD A:HEM215 3.4 24.5 1.0 CHC A:HEM215 3.4 24.9 1.0 CHB A:HEM215 3.5 25.1 1.0 ND1 A:HIS92 4.1 25.2 1.0 C3D A:HEM215 4.2 23.1 1.0 C2D A:HEM215 4.2 23.9 1.0 CG A:HIS92 4.3 23.3 1.0 ND1 A:HIS179 4.3 25.9 1.0 C2C A:HEM215 4.3 20.1 1.0 C3C A:HEM215 4.3 21.1 1.0 C2A A:HEM215 4.3 25.2 1.0 C2B A:HEM215 4.3 28.1 1.0 C3B A:HEM215 4.3 27.3 1.0 C3A A:HEM215 4.3 24.6 1.0 CG A:HIS179 4.3 24.5 1.0 O A:HOH226 4.8 33.9 1.0

Iron binding site 4 out of 4 in the Reduced State of Cytochrome C554 From Nitrosomonas Europaea


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Reduced State of Cytochrome C554 From Nitrosomonas Europaea within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe216 b:24.9 occ:1.00 FE A:HEM216 0.0 24.9 1.0 ND A:HEM216 2.0 28.1 1.0 NA A:HEM216 2.0 30.4 1.0 NC A:HEM216 2.0 28.6 1.0 NB A:HEM216 2.0 31.1 1.0 NE2 A:HIS27 2.1 21.0 1.0 NE2 A:HIS138 2.1 18.5 1.0 CE1 A:HIS27 2.9 25.6 1.0 CE1 A:HIS138 3.0 21.4 1.0 C4A A:HEM216 3.0 33.3 1.0 C4C A:HEM216 3.0 32.0 1.0 C1A A:HEM216 3.0 33.2 1.0 C1D A:HEM216 3.0 32.6 1.0 C4D A:HEM216 3.0 33.9 1.0 C1B A:HEM216 3.0 35.2 1.0 C1C A:HEM216 3.1 33.6 1.0 C4B A:HEM216 3.1 34.9 1.0 CD2 A:HIS138 3.1 20.6 1.0 CD2 A:HIS27 3.2 26.6 1.0 CHB A:HEM216 3.4 35.7 1.0 CHD A:HEM216 3.4 32.3 1.0 CHA A:HEM216 3.4 37.2 1.0 CHC A:HEM216 3.5 35.7 1.0 ND1 A:HIS138 4.1 18.5 1.0 ND1 A:HIS27 4.1 21.6 1.0 CG A:HIS138 4.2 17.5 1.0 C2A A:HEM216 4.2 36.4 1.0 C3A A:HEM216 4.2 36.0 1.0 CG A:HIS27 4.3 25.2 1.0 C3D A:HEM216 4.3 33.6 1.0 C2D A:HEM216 4.3 32.5 1.0 C3C A:HEM216 4.3 33.5 1.0 C2B A:HEM216 4.3 35.9 1.0 C2C A:HEM216 4.3 37.2 1.0 C3B A:HEM216 4.3 33.8 1.0

T.M.Iverson, D.M.Arciero, A.B.Hooper, D.C.Rees. High-Resolution Structures of the Oxidized and Reduced States of Cytochrome C554 From Nitrosomonas Europaea. J.Biol.Inorg.Chem. V. 6 390 2001.
ISSN: ISSN 0949-8257
PubMed: 11372197
DOI: 10.1007/S007750100213