Iron in PDB 8a1v: Sodium Pumping Nadh-Quinone Oxidoreductase with Substrate Q2

All present enzymatic activity of Sodium Pumping Nadh-Quinone Oxidoreductase with Substrate Q2:
7.2.1.1;

The structure of Sodium Pumping Nadh-Quinone Oxidoreductase with Substrate Q2 also contains other interesting chemical elements:

Sodium

(Na)

2 atoms

The binding sites of Iron atom in the Sodium Pumping Nadh-Quinone Oxidoreductase with Substrate Q2 (pdb code 8a1v). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 4 binding sites of Iron where determined in the Sodium Pumping Nadh-Quinone Oxidoreductase with Substrate Q2, PDB code: 8a1v:
Jump to Iron binding site number: 1; 2; 3; 4;

Iron binding site 1 out of 4 in the Sodium Pumping Nadh-Quinone Oxidoreductase with Substrate Q2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of Sodium Pumping Nadh-Quinone Oxidoreductase with Substrate Q2 within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe202 b:53.0 occ:1.00 FE1 E:FES202 0.0 53.0 1.0 S1 E:FES202 2.2 42.4 1.0 S2 E:FES202 2.2 36.2 1.0 SG E:CYS26 2.3 4.7 1.0 SG D:CYS112 2.3 17.1 1.0 FE2 E:FES202 2.7 55.5 1.0 HB2 E:CYS26 2.7 4.8 1.0 CB E:CYS26 3.1 2.9 1.0 H D:CYS112 3.2 18.3 1.0 H D:GLY27 3.4 16.5 1.0 H E:CYS26 3.5 6.4 1.0 HB2 D:CYS112 3.5 18.6 1.0 CB D:CYS112 3.6 21.2 1.0 HB3 E:CYS26 3.6 4.9 1.0 HA D:LEU26 3.9 18.8 1.0 N D:CYS112 4.0 17.7 1.0 H D:VAL28 4.1 14.2 1.0 N D:GLY27 4.1 14.0 1.0 N E:CYS26 4.2 3.3 1.0 CA E:CYS26 4.3 3.7 1.0 HB3 D:CYS112 4.3 19.0 1.0 SG D:CYS29 4.3 12.5 1.0 HA D:ASN111 4.4 16.6 1.0 CA D:CYS112 4.4 13.6 1.0 H D:CYS29 4.5 12.6 1.0 HA2 D:GLY27 4.5 16.2 1.0 SG E:CYS120 4.5 26.4 1.0 HB2 E:CYS120 4.6 9.7 1.0 O D:THR110 4.7 17.1 1.0 HD23 D:LEU26 4.7 18.7 1.0 HA E:CYS26 4.8 5.0 1.0 N D:VAL28 4.8 11.6 1.0 CA D:LEU26 4.8 22.2 1.0 CA D:GLY27 4.9 16.0 1.0 HA D:CYS112 4.9 17.6 1.0 H E:THR27 4.9 6.1 1.0 C D:LEU26 5.0 15.8 1.0 HB D:VAL28 5.0 14.5 1.0

Iron binding site 2 out of 4 in the Sodium Pumping Nadh-Quinone Oxidoreductase with Substrate Q2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of Sodium Pumping Nadh-Quinone Oxidoreductase with Substrate Q2 within 5.0Å range: probe atom residue distance (Å) B Occ E:Fe202 b:55.5 occ:1.00 FE2 E:FES202 0.0 55.5 1.0 S2 E:FES202 2.2 36.2 1.0 S1 E:FES202 2.2 42.4 1.0 SG D:CYS29 2.3 12.5 1.0 SG E:CYS120 2.3 26.4 1.0 HB2 E:CYS120 2.6 9.7 1.0 FE1 E:FES202 2.7 53.0 1.0 CB E:CYS120 2.9 9.9 1.0 HB2 D:CYS29 3.2 13.0 1.0 HB3 E:CYS120 3.3 10.7 1.0 CB D:CYS29 3.4 10.8 1.0 H E:GLY24 3.6 7.7 1.0 H D:CYS29 3.7 12.6 1.0 HB3 D:CYS29 4.0 12.2 1.0 H E:CYS120 4.0 11.2 1.0 H E:MET25 4.1 5.9 1.0 H E:CYS26 4.2 6.4 1.0 HA2 E:GLY24 4.2 6.6 1.0 HA D:ASN111 4.2 16.6 1.0 CA E:CYS120 4.3 10.8 1.0 N E:GLY24 4.3 5.1 1.0 SG E:CYS26 4.4 4.7 1.0 N D:CYS29 4.4 13.6 1.0 H D:CYS112 4.4 18.3 1.0 SG D:CYS112 4.5 17.1 1.0 CA D:CYS29 4.5 11.1 1.0 N E:CYS120 4.6 14.4 1.0 HA E:CYS120 4.6 10.7 1.0 CA E:GLY24 4.7 4.6 1.0 O D:THR110 4.7 17.1 1.0 N E:MET25 4.7 6.3 1.0 HB2 E:CYS26 4.7 4.8 1.0 HA E:LEU23 4.7 9.0 1.0 H D:VAL28 4.8 14.2 1.0 HB2 E:MET25 4.9 4.8 1.0 HA2 D:GLY27 4.9 16.2 1.0 HG1 D:THR110 5.0 13.7 1.0 H D:GLY27 5.0 16.5 1.0

Iron binding site 3 out of 4 in the Sodium Pumping Nadh-Quinone Oxidoreductase with Substrate Q2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of Sodium Pumping Nadh-Quinone Oxidoreductase with Substrate Q2 within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe1502 b:59.3 occ:1.00 FE1 F:FES1502 0.0 59.3 1.0 S2 F:FES1502 2.2 41.9 1.0 S1 F:FES1502 2.2 50.5 1.0 SG F:CYS76 2.3 43.2 1.0 SG F:CYS70 2.3 37.5 1.0 FE2 F:FES1502 2.7 70.7 1.0 HB3 F:CYS76 2.8 33.8 1.0 CB F:CYS76 3.1 37.7 1.0 H F:CYS76 3.1 33.1 1.0 H F:GLY74 3.3 28.1 1.0 H F:GLY77 3.3 31.0 1.0 H F:CYS70 3.4 30.7 1.0 H F:GLY72 3.6 28.0 1.0 N F:CYS76 3.7 35.4 1.0 CB F:CYS70 3.8 31.0 1.0 CA F:CYS76 3.8 35.7 1.0 H F:SER75 3.9 29.4 1.0 HB2 F:CYS76 3.9 34.1 1.0 HB3 F:CYS70 3.9 30.9 1.0 N F:GLY77 3.9 30.5 1.0 H F:GLN78 4.0 35.4 1.0 H F:GLY73 4.0 25.9 1.0 N F:GLY74 4.0 27.2 1.0 HA F:SER68 4.1 33.5 1.0 N F:CYS70 4.1 28.3 1.0 HA2 F:GLY74 4.3 27.6 1.0 HA2 F:GLY72 4.3 27.9 1.0 C F:CYS76 4.3 32.9 1.0 N F:GLY72 4.3 27.8 1.0 H F:CYS79 4.3 35.0 1.0 N F:SER75 4.3 30.1 1.0 HB3 F:CYS79 4.3 35.8 1.0 HB2 F:SER68 4.4 33.6 1.0 N F:GLY73 4.4 28.1 1.0 SG F:CYS79 4.4 39.9 1.0 CA F:CYS70 4.4 30.1 1.0 SG F:CYS111 4.4 32.5 1.0 H F:ALA69 4.4 32.2 1.0 H F:GLY71 4.5 28.2 1.0 HB2 F:CYS70 4.5 30.6 1.0 CA F:GLY74 4.5 28.5 1.0 HB2 F:GLN78 4.6 36.0 1.0 N F:GLN78 4.7 34.1 1.0 CA F:GLY72 4.7 29.7 1.0 HB3 F:SER68 4.7 32.9 1.0 N F:GLY71 4.7 29.4 1.0 C F:SER75 4.7 31.7 1.0 HA F:CYS76 4.7 33.5 1.0 C F:GLY74 4.7 30.3 1.0 N F:ALA69 4.7 34.7 1.0 C F:CYS70 4.7 31.7 1.0 CA F:SER68 4.8 34.6 1.0 C F:GLY72 4.8 30.1 1.0 CB F:SER68 4.8 34.9 1.0 HB3 F:CYS111 4.9 30.6 1.0 CB F:CYS79 4.9 37.5 1.0 C F:SER68 5.0 35.3 1.0 N F:CYS79 5.0 31.7 1.0

Iron binding site 4 out of 4 in the Sodium Pumping Nadh-Quinone Oxidoreductase with Substrate Q2


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of Sodium Pumping Nadh-Quinone Oxidoreductase with Substrate Q2 within 5.0Å range: probe atom residue distance (Å) B Occ F:Fe1502 b:70.7 occ:1.00 FE2 F:FES1502 0.0 70.7 1.0 S2 F:FES1502 2.2 41.9 1.0 S1 F:FES1502 2.2 50.5 1.0 SG F:CYS79 2.3 39.9 1.0 SG F:CYS111 2.3 32.5 1.0 FE1 F:FES1502 2.7 59.3 1.0 HB3 F:CYS111 2.8 30.6 1.0 HB3 F:CYS79 3.1 35.8 1.0 CB F:CYS111 3.1 31.3 1.0 CB F:CYS79 3.3 37.5 1.0 H F:CYS111 3.5 31.1 1.0 HA2 F:GLY74 3.7 27.6 1.0 H F:GLY74 3.7 28.1 1.0 HA2 F:GLY72 3.7 27.9 1.0 HB2 F:CYS111 3.8 30.0 1.0 HB2 F:CYS79 3.8 35.6 1.0 HB3 F:LEU109 3.8 31.4 1.0 H F:CYS79 3.9 35.0 1.0 HG2 F:GLN112 3.9 30.0 1.0 HE21 F:GLN112 4.1 29.2 1.0 H F:GLY77 4.2 31.0 1.0 N F:CYS111 4.2 34.5 1.0 CA F:CYS111 4.2 34.1 1.0 H F:GLY72 4.2 28.0 1.0 N F:GLY74 4.4 27.2 1.0 SG F:CYS76 4.4 43.2 1.0 CA F:GLY74 4.4 28.5 1.0 HD22 F:LEU109 4.4 31.4 1.0 SG F:CYS70 4.4 37.5 1.0 H F:GLN112 4.5 29.7 1.0 N F:CYS79 4.5 31.7 1.0 CA F:CYS79 4.5 37.8 1.0 CA F:GLY72 4.5 29.7 1.0 HD13 F:LEU109 4.5 31.9 1.0 H F:CYS76 4.6 33.1 1.0 NE2 F:GLN112 4.7 29.5 1.0 CB F:LEU109 4.8 32.1 1.0 N F:GLY72 4.8 27.8 1.0 HB3 F:SER68 4.8 32.9 1.0 CG F:GLN112 4.9 30.7 1.0 N F:GLN112 4.9 30.7 1.0 C F:GLY72 4.9 30.1 1.0 C F:CYS111 4.9 31.5 1.0 N F:GLY77 4.9 30.5 1.0

J.-L.Hau, J.-L.Hau, S.Kaltwasser, J.Vonck, G.Fritz, J.Steuber. N/A N/A.