Iron in PDB 1fft: The Structure of Ubiquinol Oxidase From Escherichia Coli

The structure of The Structure of Ubiquinol Oxidase From Escherichia Coli, PDB code: 1fft was solved by J.Abramson, S.Riistama, G.Larsson, A.Jasaitis, M.Svensson-Ek, A.Puustinen, S.Iwata, M.Wikstrom, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	40.00 / 3.50
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	92.100, 372.500, 232.700, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The structure of The Structure of Ubiquinol Oxidase From Escherichia Coli also contains other interesting chemical elements:

Copper

(Cu)

2 atoms

The binding sites of Iron atom in the The Structure of Ubiquinol Oxidase From Escherichia Coli (pdb code 1fft). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the The Structure of Ubiquinol Oxidase From Escherichia Coli, PDB code: 1fft:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the The Structure of Ubiquinol Oxidase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of The Structure of Ubiquinol Oxidase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1001 b:29.5 occ:1.00 FE A:HEM1001 0.0 29.5 1.0 ND A:HEM1001 1.9 29.5 1.0 NA A:HEM1001 2.0 29.5 1.0 NC A:HEM1001 2.0 29.5 1.0 NB A:HEM1001 2.0 29.5 1.0 NE2 A:HIS106 2.2 29.5 1.0 NE2 A:HIS421 2.2 29.5 1.0 C1D A:HEM1001 3.0 29.5 1.0 C4D A:HEM1001 3.0 29.5 1.0 C1A A:HEM1001 3.0 29.5 1.0 C4A A:HEM1001 3.0 29.5 1.0 C4C A:HEM1001 3.0 29.5 1.0 C1C A:HEM1001 3.1 29.5 1.0 C1B A:HEM1001 3.1 29.5 1.0 C4B A:HEM1001 3.1 29.5 1.0 CD2 A:HIS106 3.1 29.5 1.0 CD2 A:HIS421 3.2 29.5 1.0 CE1 A:HIS106 3.2 29.5 1.0 CE1 A:HIS421 3.2 29.5 1.0 CHA A:HEM1001 3.4 29.5 1.0 CHD A:HEM1001 3.4 29.5 1.0 CHB A:HEM1001 3.4 29.5 1.0 CHC A:HEM1001 3.4 29.5 1.0 C2D A:HEM1001 4.2 29.5 1.0 C3D A:HEM1001 4.2 29.5 1.0 C3A A:HEM1001 4.2 29.5 1.0 C2A A:HEM1001 4.2 29.5 1.0 C2C A:HEM1001 4.3 29.5 1.0 C3B A:HEM1001 4.3 29.5 1.0 C3C A:HEM1001 4.3 29.5 1.0 ND1 A:HIS106 4.3 29.5 1.0 CG A:HIS106 4.3 29.5 1.0 C2B A:HEM1001 4.3 29.5 1.0 ND1 A:HIS421 4.3 29.5 1.0 CG A:HIS421 4.3 29.5 1.0

Iron binding site 2 out of 4 in the The Structure of Ubiquinol Oxidase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of The Structure of Ubiquinol Oxidase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1002 b:29.5 occ:1.00 FE A:HEO1002 0.0 29.5 1.0 NA A:HEO1002 2.0 29.5 1.0 NB A:HEO1002 2.0 29.5 1.0 ND A:HEO1002 2.0 29.5 1.0 NC A:HEO1002 2.0 29.5 1.0 NE2 A:HIS419 2.2 29.5 1.0 C4A A:HEO1002 3.0 29.5 1.0 C1B A:HEO1002 3.0 29.5 1.0 C1A A:HEO1002 3.0 29.5 1.0 C4B A:HEO1002 3.0 29.5 1.0 C4D A:HEO1002 3.0 29.5 1.0 C1C A:HEO1002 3.0 29.5 1.0 C1D A:HEO1002 3.1 29.5 1.0 C4C A:HEO1002 3.1 29.5 1.0 CD2 A:HIS419 3.2 29.5 1.0 CE1 A:HIS419 3.2 29.5 1.0 CHB A:HEO1002 3.4 29.5 1.0 CHA A:HEO1002 3.4 29.5 1.0 CHC A:HEO1002 3.4 29.5 1.0 CHD A:HEO1002 3.4 29.5 1.0 C3A A:HEO1002 4.2 29.5 1.0 C2A A:HEO1002 4.2 29.5 1.0 C3B A:HEO1002 4.2 29.5 1.0 C2B A:HEO1002 4.2 29.5 1.0 C3D A:HEO1002 4.3 29.5 1.0 C2D A:HEO1002 4.3 29.5 1.0 C2C A:HEO1002 4.3 29.5 1.0 C3C A:HEO1002 4.3 29.5 1.0 ND1 A:HIS419 4.3 29.5 1.0 CG A:HIS419 4.4 29.5 1.0 CB A:PHE420 4.9 29.5 1.0

Iron binding site 3 out of 4 in the The Structure of Ubiquinol Oxidase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of The Structure of Ubiquinol Oxidase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe1001 b:29.5 occ:1.00 FE F:HEM1001 0.0 29.5 1.0 ND F:HEM1001 2.0 29.5 1.0 NA F:HEM1001 2.0 29.5 1.0 NB F:HEM1001 2.0 29.5 1.0 NC F:HEM1001 2.0 29.5 1.0 NE2 F:HIS106 2.2 29.5 1.0 NE2 F:HIS421 2.2 29.5 1.0 C1D F:HEM1001 3.0 29.5 1.0 C4A F:HEM1001 3.0 29.5 1.0 C4D F:HEM1001 3.0 29.5 1.0 C1A F:HEM1001 3.0 29.5 1.0 C1C F:HEM1001 3.0 29.5 1.0 C4C F:HEM1001 3.0 29.5 1.0 C4B F:HEM1001 3.0 29.5 1.0 C1B F:HEM1001 3.0 29.5 1.0 CD2 F:HIS106 3.1 29.5 1.0 CE1 F:HIS106 3.2 29.5 1.0 CD2 F:HIS421 3.2 29.5 1.0 CE1 F:HIS421 3.2 29.5 1.0 CHD F:HEM1001 3.4 29.5 1.0 CHB F:HEM1001 3.4 29.5 1.0 CHA F:HEM1001 3.4 29.5 1.0 CHC F:HEM1001 3.4 29.5 1.0 C2D F:HEM1001 4.2 29.5 1.0 C3A F:HEM1001 4.2 29.5 1.0 C3D F:HEM1001 4.2 29.5 1.0 C3B F:HEM1001 4.3 29.5 1.0 C2A F:HEM1001 4.3 29.5 1.0 C2C F:HEM1001 4.3 29.5 1.0 C2B F:HEM1001 4.3 29.5 1.0 C3C F:HEM1001 4.3 29.5 1.0 CG F:HIS106 4.3 29.5 1.0 ND1 F:HIS106 4.3 29.5 1.0 ND1 F:HIS421 4.3 29.5 1.0 CG F:HIS421 4.4 29.5 1.0

Iron binding site 4 out of 4 in the The Structure of Ubiquinol Oxidase From Escherichia Coli


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of The Structure of Ubiquinol Oxidase From Escherichia Coli within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe1002 b:29.5 occ:1.00 FE F:HEO1002 0.0 29.5 1.0 NA F:HEO1002 2.0 29.5 1.0 NB F:HEO1002 2.0 29.5 1.0 ND F:HEO1002 2.0 29.5 1.0 NC F:HEO1002 2.0 29.5 1.0 NE2 F:HIS419 2.2 29.5 1.0 C1A F:HEO1002 3.0 29.5 1.0 C4A F:HEO1002 3.0 29.5 1.0 C1B F:HEO1002 3.0 29.5 1.0 C4D F:HEO1002 3.0 29.5 1.0 C4B F:HEO1002 3.0 29.5 1.0 C1C F:HEO1002 3.0 29.5 1.0 C1D F:HEO1002 3.0 29.5 1.0 C4C F:HEO1002 3.0 29.5 1.0 CD2 F:HIS419 3.2 29.5 1.0 CE1 F:HIS419 3.2 29.5 1.0 CHA F:HEO1002 3.4 29.5 1.0 CHB F:HEO1002 3.4 29.5 1.0 CHC F:HEO1002 3.4 29.5 1.0 CHD F:HEO1002 3.4 29.5 1.0 C3A F:HEO1002 4.2 29.5 1.0 C3B F:HEO1002 4.2 29.5 1.0 C2A F:HEO1002 4.2 29.5 1.0 C3D F:HEO1002 4.3 29.5 1.0 C2B F:HEO1002 4.3 29.5 1.0 C2D F:HEO1002 4.3 29.5 1.0 C2C F:HEO1002 4.3 29.5 1.0 C3C F:HEO1002 4.3 29.5 1.0 ND1 F:HIS419 4.3 29.5 1.0 CG F:HIS419 4.4 29.5 1.0 CB F:PHE420 4.9 29.5 1.0

J.Abramson, S.Riistama, G.Larsson, A.Jasaitis, M.Svensson-Ek, L.Laakkonen, A.Puustinen, S.Iwata, M.Wikstrom. The Structure of the Ubiquinol Oxidase From Escherichia Coli and Its Ubiquinone Binding Site. Nat.Struct.Biol. V. 7 910 2000.
ISSN: ISSN 1072-8368
PubMed: 11017202
DOI: 10.1038/82824