Iron in PDB 2vr0: Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor

All present enzymatic activity of Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor:
1.7.2.2;

The structure of Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor, PDB code: 2vr0 was solved by M.L.Rodrigues, M.Archer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	154.30 / 2.80
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	80.102, 189.115, 263.460, 90.00, 90.00, 90.00
R / Rfree (%)	22 / 26.1

The structure of Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor also contains other interesting chemical elements:

Calcium

(Ca)

8 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 28;

Binding sites:

The binding sites of Iron atom in the Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor (pdb code 2vr0). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 28 binding sites of Iron where determined in the Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor, PDB code: 2vr0:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 28 in the Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1001 b:22.2 occ:1.00 FE A:HEC1001 0.0 22.2 1.0 NB A:HEC1001 2.0 22.0 1.0 NA A:HEC1001 2.0 23.6 1.0 ND A:HEC1001 2.1 21.0 1.0 NC A:HEC1001 2.1 21.8 1.0 NZ A:LYS151 2.3 24.9 1.0 O A:HOH2023 2.9 12.6 1.0 C4A A:HEC1001 3.0 24.2 1.0 C4B A:HEC1001 3.0 22.5 1.0 C1B A:HEC1001 3.0 23.6 1.0 C1A A:HEC1001 3.0 24.2 1.0 C4D A:HEC1001 3.1 21.8 1.0 C1C A:HEC1001 3.1 21.1 1.0 C1D A:HEC1001 3.1 21.0 1.0 C4C A:HEC1001 3.2 20.0 1.0 CE A:LYS151 3.2 24.8 1.0 CHB A:HEC1001 3.4 23.6 1.0 CHC A:HEC1001 3.4 21.6 1.0 CHA A:HEC1001 3.4 21.8 1.0 CHD A:HEC1001 3.5 21.0 1.0 NE2 A:HIS298 4.2 24.1 1.0 C3B A:HEC1001 4.2 24.0 1.0 C3A A:HEC1001 4.2 24.4 1.0 C2B A:HEC1001 4.2 24.4 1.0 C2A A:HEC1001 4.2 25.1 1.0 C3D A:HEC1001 4.3 21.5 1.0 C2C A:HEC1001 4.3 19.0 1.0 C2D A:HEC1001 4.3 20.5 1.0 C3C A:HEC1001 4.4 19.3 1.0 O A:HOH2010 4.4 7.4 1.0 CD A:LYS151 4.6 24.3 1.0 CE1 A:HIS298 5.0 24.2 1.0

Iron binding site 2 out of 28 in the Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1002 b:22.9 occ:1.00 FE A:HEC1002 0.0 22.9 1.0 NC A:HEC1002 2.0 22.5 1.0 NE2 A:HIS335 2.0 22.3 1.0 NB A:HEC1002 2.0 21.8 1.0 NE2 A:HIS191 2.0 24.6 1.0 ND A:HEC1002 2.0 23.0 1.0 NA A:HEC1002 2.0 22.9 1.0 CE1 A:HIS191 2.8 25.0 1.0 CE1 A:HIS335 2.9 22.4 1.0 C4C A:HEC1002 3.0 22.9 1.0 C1C A:HEC1002 3.0 22.1 1.0 C1B A:HEC1002 3.0 22.1 1.0 C4B A:HEC1002 3.0 21.7 1.0 C4D A:HEC1002 3.1 24.2 1.0 C4A A:HEC1002 3.1 21.7 1.0 C1D A:HEC1002 3.1 24.0 1.0 C1A A:HEC1002 3.1 23.3 1.0 CD2 A:HIS335 3.1 23.2 1.0 CD2 A:HIS191 3.2 24.3 1.0 CHB A:HEC1002 3.4 21.9 1.0 CHD A:HEC1002 3.4 23.0 1.0 CHC A:HEC1002 3.4 21.6 1.0 CHA A:HEC1002 3.4 23.0 1.0 ND1 A:HIS191 4.0 25.3 1.0 ND1 A:HIS335 4.0 22.5 1.0 CG A:HIS335 4.2 23.0 1.0 CG A:HIS191 4.2 24.5 1.0 C3C A:HEC1002 4.2 22.3 1.0 C2C A:HEC1002 4.2 22.4 1.0 C2B A:HEC1002 4.3 21.4 1.0 C3B A:HEC1002 4.3 22.0 1.0 C3A A:HEC1002 4.3 22.6 1.0 C2A A:HEC1002 4.3 22.7 1.0 C3D A:HEC1002 4.3 24.6 1.0 C2D A:HEC1002 4.3 23.7 1.0 CE A:MET321 4.4 23.3 1.0

Iron binding site 3 out of 28 in the Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1003 b:13.0 occ:1.00 FE A:HEC1003 0.0 13.0 1.0 NE2 A:HIS121 1.9 23.8 1.0 ND A:HEC1003 1.9 11.3 1.0 NA A:HEC1003 2.0 12.5 1.0 NC A:HEC1003 2.0 13.0 1.0 NB A:HEC1003 2.0 12.4 1.0 NE2 A:HIS233 2.3 23.0 1.0 CD2 A:HIS121 2.9 22.4 1.0 C1D A:HEC1003 2.9 13.6 1.0 CE1 A:HIS121 2.9 23.7 1.0 C4D A:HEC1003 2.9 12.7 1.0 C4C A:HEC1003 3.0 13.6 1.0 C1B A:HEC1003 3.0 13.8 1.0 C4A A:HEC1003 3.0 12.5 1.0 C1A A:HEC1003 3.0 13.1 1.0 C1C A:HEC1003 3.1 13.5 1.0 C4B A:HEC1003 3.1 11.7 1.0 CD2 A:HIS233 3.2 23.3 1.0 CE1 A:HIS233 3.3 22.6 1.0 CHD A:HEC1003 3.3 13.3 1.0 CHA A:HEC1003 3.4 13.5 1.0 CHB A:HEC1003 3.4 13.1 1.0 CHC A:HEC1003 3.5 13.3 1.0 ND1 A:HIS121 4.0 22.9 1.0 CG A:HIS121 4.0 22.7 1.0 C2D A:HEC1003 4.2 13.7 1.0 C3D A:HEC1003 4.2 14.0 1.0 C3A A:HEC1003 4.2 14.3 1.0 C2B A:HEC1003 4.2 12.6 1.0 C3C A:HEC1003 4.3 13.2 1.0 C2A A:HEC1003 4.3 14.4 1.0 C2C A:HEC1003 4.3 12.5 1.0 C3B A:HEC1003 4.3 11.2 1.0 CG A:HIS233 4.4 24.0 1.0 ND1 A:HIS233 4.4 23.1 1.0 CMD A:HEC1001 4.9 20.5 1.0

Iron binding site 4 out of 28 in the Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1004 b:7.0 occ:1.00 FE A:HEC1004 0.0 7.0 1.0 NA A:HEC1004 1.9 4.4 1.0 NB A:HEC1004 2.0 6.9 1.0 ND A:HEC1004 2.0 3.9 1.0 NC A:HEC1004 2.0 6.2 1.0 NE2 A:HIS434 2.1 24.1 1.0 NE2 A:HIS320 2.2 22.4 1.0 C4A A:HEC1004 2.9 6.0 1.0 C1B A:HEC1004 3.0 9.3 1.0 CE1 A:HIS434 3.0 23.7 1.0 C1A A:HEC1004 3.0 4.6 1.0 C4C A:HEC1004 3.0 7.4 1.0 C1D A:HEC1004 3.0 5.2 1.0 C4D A:HEC1004 3.0 5.3 1.0 CD2 A:HIS320 3.1 22.9 1.0 C4B A:HEC1004 3.1 9.2 1.0 C1C A:HEC1004 3.1 8.2 1.0 CHB A:HEC1004 3.3 7.7 1.0 CE1 A:HIS320 3.3 21.7 1.0 CD2 A:HIS434 3.3 23.9 1.0 CHD A:HEC1004 3.3 7.4 1.0 CHA A:HEC1004 3.4 5.5 1.0 CHC A:HEC1004 3.5 9.2 1.0 ND1 A:HIS434 4.1 22.4 1.0 C3A A:HEC1004 4.2 6.2 1.0 C2A A:HEC1004 4.2 6.8 1.0 C2B A:HEC1004 4.2 10.3 1.0 C3C A:HEC1004 4.2 7.9 1.0 C2D A:HEC1004 4.3 5.4 1.0 CG A:HIS320 4.3 23.3 1.0 C3D A:HEC1004 4.3 7.1 1.0 C3B A:HEC1004 4.3 9.7 1.0 C2C A:HEC1004 4.3 7.4 1.0 ND1 A:HIS320 4.3 22.4 1.0 CG A:HIS434 4.3 23.6 1.0

Iron binding site 5 out of 28 in the Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe1005 b:14.7 occ:1.00 FE A:HEC1005 0.0 14.7 1.0 NA A:HEC1005 1.9 15.6 1.0 NE2 A:HIS353 1.9 21.9 1.0 NC A:HEC1005 2.0 15.3 1.0 NB A:HEC1005 2.1 15.5 1.0 NE2 A:HIS309 2.1 20.9 1.0 ND A:HEC1005 2.1 17.6 1.0 CE1 A:HIS353 2.8 22.6 1.0 C4A A:HEC1005 3.0 15.8 1.0 C1A A:HEC1005 3.0 16.9 1.0 C4C A:HEC1005 3.0 14.3 1.0 C1B A:HEC1005 3.0 15.1 1.0 CE1 A:HIS309 3.0 22.4 1.0 C1C A:HEC1005 3.0 15.4 1.0 CD2 A:HIS353 3.1 22.9 1.0 C4D A:HEC1005 3.1 17.7 1.0 C1D A:HEC1005 3.1 17.2 1.0 C4B A:HEC1005 3.1 14.2 1.0 CD2 A:HIS309 3.1 22.4 1.0 CHB A:HEC1005 3.3 15.3 1.0 CHD A:HEC1005 3.4 16.3 1.0 CHA A:HEC1005 3.4 16.6 1.0 CHC A:HEC1005 3.5 14.6 1.0 ND1 A:HIS353 3.9 21.9 1.0 CG A:HIS353 4.1 22.7 1.0 ND1 A:HIS309 4.2 22.5 1.0 C3A A:HEC1005 4.2 16.2 1.0 C2A A:HEC1005 4.2 16.9 1.0 C2C A:HEC1005 4.2 15.1 1.0 C3C A:HEC1005 4.2 14.9 1.0 CG A:HIS309 4.3 23.1 1.0 C2B A:HEC1005 4.3 15.0 1.0 C3B A:HEC1005 4.3 14.6 1.0 C3D A:HEC1005 4.3 17.8 1.0 C2D A:HEC1005 4.3 17.0 1.0 CBC A:HEC1004 5.0 11.8 1.0

Iron binding site 6 out of 28 in the Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1001 b:15.2 occ:1.00 FE B:HEC1001 0.0 15.2 1.0 NC B:HEC1001 2.0 14.6 1.0 NA B:HEC1001 2.0 13.4 1.0 NB B:HEC1001 2.1 15.0 1.0 O B:HOH2041 2.1 21.9 1.0 ND B:HEC1001 2.1 14.3 1.0 NZ B:LYS151 2.2 23.7 1.0 C1A B:HEC1001 3.0 13.4 1.0 C1C B:HEC1001 3.0 14.2 1.0 C4B B:HEC1001 3.0 15.2 1.0 C4C B:HEC1001 3.1 14.1 1.0 C1D B:HEC1001 3.1 12.8 1.0 C4D B:HEC1001 3.1 12.8 1.0 C4A B:HEC1001 3.1 13.4 1.0 C1B B:HEC1001 3.1 16.6 1.0 CE B:LYS151 3.2 24.8 1.0 CHC B:HEC1001 3.4 14.7 1.0 CHD B:HEC1001 3.4 13.1 1.0 CHA B:HEC1001 3.4 11.8 1.0 CHB B:HEC1001 3.5 14.0 1.0 O B:HOH2017 4.1 8.0 1.0 C2C B:HEC1001 4.3 13.7 1.0 C2A B:HEC1001 4.3 14.1 1.0 C3B B:HEC1001 4.3 15.8 1.0 C3C B:HEC1001 4.3 14.8 1.0 C2D B:HEC1001 4.3 9.5 1.0 C3A B:HEC1001 4.3 13.5 1.0 C2B B:HEC1001 4.3 17.0 1.0 C3D B:HEC1001 4.3 10.5 1.0 CD B:LYS151 4.5 25.4 1.0 CE1 B:HIS298 4.6 27.0 1.0 NE2 B:HIS298 4.6 26.6 1.0

Iron binding site 7 out of 28 in the Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1002 b:21.2 occ:1.00 FE B:HEC1002 0.0 21.2 1.0 NC B:HEC1002 2.0 22.0 1.0 NE2 B:HIS191 2.0 21.6 1.0 NB B:HEC1002 2.0 21.8 1.0 ND B:HEC1002 2.1 20.1 1.0 NE2 B:HIS335 2.1 22.4 1.0 NA B:HEC1002 2.1 22.1 1.0 CE1 B:HIS191 3.0 21.8 1.0 C1C B:HEC1002 3.0 22.3 1.0 CD2 B:HIS191 3.0 21.9 1.0 CD2 B:HIS335 3.0 22.6 1.0 C4C B:HEC1002 3.0 21.4 1.0 C4B B:HEC1002 3.0 22.5 1.0 C4D B:HEC1002 3.1 19.8 1.0 C1A B:HEC1002 3.1 22.3 1.0 C1B B:HEC1002 3.1 22.4 1.0 C1D B:HEC1002 3.1 19.9 1.0 C4A B:HEC1002 3.1 22.1 1.0 CE1 B:HIS335 3.1 22.2 1.0 CHC B:HEC1002 3.3 22.5 1.0 CHD B:HEC1002 3.4 20.3 1.0 CHA B:HEC1002 3.4 20.4 1.0 CHB B:HEC1002 3.5 22.6 1.0 ND1 B:HIS191 4.1 21.9 1.0 CG B:HIS191 4.1 22.6 1.0 CG B:HIS335 4.2 22.7 1.0 C3C B:HEC1002 4.2 21.8 1.0 C2C B:HEC1002 4.2 21.6 1.0 ND1 B:HIS335 4.2 22.2 1.0 C3B B:HEC1002 4.3 22.9 1.0 C2A B:HEC1002 4.3 23.7 1.0 C2B B:HEC1002 4.3 22.6 1.0 C3D B:HEC1002 4.3 19.2 1.0 C3A B:HEC1002 4.3 23.3 1.0 C2D B:HEC1002 4.3 18.9 1.0 CE B:MET321 4.6 20.4 1.0

Iron binding site 8 out of 28 in the Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1003 b:7.0 occ:1.00 FE B:HEC1003 0.0 7.0 1.0 NC B:HEC1003 1.9 4.7 1.0 NE2 B:HIS121 2.0 22.1 1.0 NA B:HEC1003 2.0 7.5 1.0 NB B:HEC1003 2.0 5.7 1.0 ND B:HEC1003 2.1 5.1 1.0 NE2 B:HIS233 2.1 24.1 1.0 C4C B:HEC1003 2.9 6.1 1.0 CE1 B:HIS233 2.9 24.9 1.0 CE1 B:HIS121 2.9 22.0 1.0 C1B B:HEC1003 3.0 7.1 1.0 C4A B:HEC1003 3.0 9.6 1.0 CD2 B:HIS121 3.0 22.4 1.0 C1D B:HEC1003 3.0 5.7 1.0 C1C B:HEC1003 3.0 5.2 1.0 C1A B:HEC1003 3.1 8.6 1.0 C4B B:HEC1003 3.1 5.7 1.0 C4D B:HEC1003 3.2 6.3 1.0 CD2 B:HIS233 3.2 23.3 1.0 CHD B:HEC1003 3.2 7.0 1.0 CHB B:HEC1003 3.3 9.0 1.0 CHC B:HEC1003 3.5 6.3 1.0 CHA B:HEC1003 3.5 7.8 1.0 ND1 B:HIS121 4.0 22.4 1.0 CG B:HIS121 4.1 22.5 1.0 ND1 B:HIS233 4.1 25.2 1.0 C3C B:HEC1003 4.1 5.1 1.0 C2C B:HEC1003 4.2 4.5 1.0 C2B B:HEC1003 4.2 6.0 1.0 C3A B:HEC1003 4.2 9.0 1.0 C2A B:HEC1003 4.2 9.5 1.0 CG B:HIS233 4.3 23.4 1.0 C2D B:HEC1003 4.3 5.0 1.0 C3B B:HEC1003 4.3 6.0 1.0 C3D B:HEC1003 4.4 5.8 1.0 O B:HOH2028 4.9 9.7 1.0

Iron binding site 9 out of 28 in the Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1004 b:3.0 occ:1.00 FE B:HEC1004 0.0 3.0 1.0 NC B:HEC1004 1.9 2.8 1.0 NB B:HEC1004 2.0 2.0 1.0 NE2 B:HIS434 2.0 17.8 1.0 ND B:HEC1004 2.0 2.0 1.0 NA B:HEC1004 2.1 3.5 1.0 NE2 B:HIS320 2.1 20.1 1.0 CE1 B:HIS434 2.8 17.2 1.0 C4C B:HEC1004 2.9 3.6 1.0 C1D B:HEC1004 2.9 2.1 1.0 C1C B:HEC1004 3.0 2.2 1.0 C1B B:HEC1004 3.0 3.6 1.0 C4B B:HEC1004 3.0 4.8 1.0 C4A B:HEC1004 3.1 5.8 1.0 CD2 B:HIS320 3.1 21.2 1.0 CE1 B:HIS320 3.1 19.4 1.0 C4D B:HEC1004 3.2 2.0 1.0 CD2 B:HIS434 3.2 19.1 1.0 C1A B:HEC1004 3.2 4.2 1.0 CHD B:HEC1004 3.2 3.5 1.0 CHB B:HEC1004 3.3 5.6 1.0 CHC B:HEC1004 3.4 3.4 1.0 CHA B:HEC1004 3.6 3.4 1.0 ND1 B:HIS434 4.0 16.3 1.0 C3C B:HEC1004 4.1 3.3 1.0 C2C B:HEC1004 4.2 2.5 1.0 CG B:HIS434 4.2 19.5 1.0 ND1 B:HIS320 4.2 20.1 1.0 C2D B:HEC1004 4.2 2.9 1.0 CG B:HIS320 4.3 21.3 1.0 C2B B:HEC1004 4.3 3.9 1.0 C3B B:HEC1004 4.3 5.4 1.0 C3D B:HEC1004 4.3 4.2 1.0 C3A B:HEC1004 4.4 5.7 1.0 C2A B:HEC1004 4.4 4.0 1.0 CB B:SER430 4.9 24.1 1.0

Iron binding site 10 out of 28 in the Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of Crystal Structure of Cytochrome C Nitrite Reductase Nrfha Complex Bound to the Hqno Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe1005 b:17.7 occ:1.00 FE B:HEC1005 0.0 17.7 1.0 NA B:HEC1005 2.0 18.0 1.0 NE2 B:HIS353 2.0 21.2 1.0 NC B:HEC1005 2.0 18.1 1.0 NB B:HEC1005 2.0 17.6 1.0 NE2 B:HIS309 2.0 23.1 1.0 ND B:HEC1005 2.1 18.0 1.0 CE1 B:HIS353 2.8 22.0 1.0 C4A B:HEC1005 3.0 19.2 1.0 C1C B:HEC1005 3.0 18.0 1.0 C1A B:HEC1005 3.0 18.7 1.0 C4C B:HEC1005 3.0 18.1 1.0 CD2 B:HIS309 3.0 23.8 1.0 C1B B:HEC1005 3.0 16.8 1.0 CE1 B:HIS309 3.0 23.5 1.0 C4B B:HEC1005 3.1 17.9 1.0 CD2 B:HIS353 3.1 22.5 1.0 C4D B:HEC1005 3.1 17.5 1.0 C1D B:HEC1005 3.1 17.8 1.0 CHB B:HEC1005 3.4 18.0 1.0 CHC B:HEC1005 3.4 18.2 1.0 CHA B:HEC1005 3.4 17.2 1.0 CHD B:HEC1005 3.4 17.6 1.0 ND1 B:HIS353 4.0 21.9 1.0 CG B:HIS353 4.1 22.6 1.0 ND1 B:HIS309 4.1 22.9 1.0 CG B:HIS309 4.2 23.8 1.0 C2C B:HEC1005 4.2 17.9 1.0 C3A B:HEC1005 4.2 19.5 1.0 C3C B:HEC1005 4.2 18.9 1.0 C2A B:HEC1005 4.2 19.8 1.0 C2B B:HEC1005 4.2 17.3 1.0 C3B B:HEC1005 4.3 17.5 1.0 C3D B:HEC1005 4.3 17.9 1.0 C2D B:HEC1005 4.3 17.1 1.0 CBC B:HEC1004 4.8 9.3 1.0

M.L.Rodrigues, K.A.Scott, M.S.P.Sansom, I.A.C.Pereira, M.Archer. Quinol Oxidation By C-Type Cytochromes: Structural Characterization of the Menaquinol Binding Site of Nrfha. J.Mol.Biol. V. 381 341 2008.
ISSN: ISSN 0022-2836
PubMed: 18597779
DOI: 10.1016/J.JMB.2008.05.066