Iron in PDB 6zgp: Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Inhibitor MMV12 (MMV020670)

All present enzymatic activity of Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Inhibitor MMV12 (MMV020670):
1.14.13.239;

The structure of Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Inhibitor MMV12 (MMV020670), PDB code: 6zgp was solved by M.Quareshy, M.Shanmugam, T.D.H.Bugg, A.Cameron, Y.Chen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	80.66 / 2.01
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	91.070, 173.770, 157.290, 90.00, 90.15, 90.00
R / Rfree (%)	21.4 / 25.5

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 20; Page 3, Binding sites: 21 - 30; Page 4, Binding sites: 31 - 36;

Binding sites:

The binding sites of Iron atom in the Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Inhibitor MMV12 (MMV020670) (pdb code 6zgp). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 36 binding sites of Iron where determined in the Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Inhibitor MMV12 (MMV020670), PDB code: 6zgp:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 36 in the Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Inhibitor MMV12 (MMV020670)


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 the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Inhibitor MMV12 (MMV020670) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe401 b:81.2 occ:1.00 NE2 A:HIS213 2.2 96.7 1.0 N1 A:QKQ403 2.2 77.4 1.0 C8 A:QKQ403 2.3 82.8 1.0 OD1 A:ASP323 2.4 0.0 1.0 NE2 A:HIS208 2.4 82.2 1.0 OD2 A:ASP323 2.5 0.8 1.0 CG A:ASP323 2.8 94.6 1.0 CD2 A:HIS213 2.9 98.3 1.0 CE1 A:HIS208 3.3 81.5 1.0 CE1 A:HIS213 3.3 98.7 1.0 C7 A:QKQ403 3.5 77.4 1.0 CD2 A:HIS208 3.5 82.9 1.0 C9 A:QKQ403 3.6 81.2 1.0 ND2 A:ASN202 3.9 52.8 1.0 CG A:HIS213 4.1 0.2 1.0 C10 A:QKQ403 4.3 79.7 1.0 CB A:ASP323 4.3 72.8 1.0 ND1 A:HIS213 4.3 99.6 1.0 OD1 A:ASN202 4.4 55.2 1.0 ND1 A:HIS208 4.4 81.5 1.0 CG A:ASN202 4.5 52.1 1.0 C6 A:QKQ403 4.5 77.2 1.0 C20 A:QKQ403 4.6 78.6 1.0 CG A:HIS208 4.6 81.9 1.0 O A:ASN202 4.6 55.8 1.0

Iron binding site 2 out of 36 in the Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Inhibitor MMV12 (MMV020670)


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 the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Inhibitor MMV12 (MMV020670) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe402 b:81.2 occ:1.00 FE1 A:FES402 0.0 81.2 1.0 S2 A:FES402 2.2 52.7 1.0 S1 A:FES402 2.2 80.2 1.0 ND1 A:HIS88 2.2 30.4 1.0 ND1 A:HIS109 2.3 43.0 1.0 CE1 A:HIS109 3.1 42.2 1.0 FE2 A:FES402 3.1 33.2 1.0 CE1 A:HIS88 3.2 35.5 1.0 CG A:HIS88 3.3 32.7 1.0 CG A:HIS109 3.4 42.6 1.0 CB A:HIS88 3.6 33.7 1.0 CB A:HIS109 3.8 42.7 1.0 N A:ARG89 3.8 35.9 1.0 CB A:TYR108 4.0 42.8 1.0 CD2 A:TYR108 4.1 40.6 1.0 CB A:ARG89 4.1 42.6 1.0 N A:HIS109 4.2 44.7 1.0 NE2 A:HIS109 4.2 44.2 1.0 CG A:TYR108 4.3 42.7 1.0 NE2 A:HIS88 4.3 30.3 1.0 CD2 A:HIS88 4.3 32.9 1.0 CD2 A:HIS109 4.4 44.3 1.0 CA A:ARG89 4.5 37.4 1.0 C A:HIS88 4.6 39.2 1.0 CA A:HIS109 4.6 45.4 1.0 SG A:CYS86 4.6 38.0 1.0 CA A:HIS88 4.6 36.7 1.0 SG A:CYS106 4.8 0.4 1.0 C A:TYR108 4.8 48.4 1.0 CG A:ARG89 4.9 46.3 1.0 CE2 A:TYR108 4.9 38.9 1.0

Iron binding site 3 out of 36 in the Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Inhibitor MMV12 (MMV020670)


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 the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Inhibitor MMV12 (MMV020670) within 5.0Å range: probe atom residue distance (Å) B Occ A:Fe402 b:33.2 occ:1.00 FE2 A:FES402 0.0 33.2 1.0 S2 A:FES402 2.2 52.7 1.0 S1 A:FES402 2.2 80.2 1.0 SG A:CYS106 2.3 0.4 1.0 SG A:CYS86 2.5 38.0 1.0 CB A:CYS86 2.9 35.7 1.0 CB A:CYS106 2.9 78.3 1.0 FE1 A:FES402 3.1 81.2 1.0 CA A:CYS86 4.4 36.5 1.0 CA A:CYS106 4.4 54.0 1.0 CB A:TYR108 4.4 42.8 1.0 CB A:HIS91 4.5 32.5 1.0 N A:HIS109 4.6 44.7 1.0 CB A:HIS88 4.6 33.7 1.0 CD2 A:LEU93 4.6 36.1 1.0 C A:CYS106 4.8 41.6 1.0 N A:TYR108 4.9 46.5 1.0 ND1 A:HIS88 4.9 30.4 1.0 N A:HIS91 4.9 28.8 1.0 N A:ARG89 4.9 35.9 1.0 CB A:TRP111 4.9 40.7 1.0 ND1 A:HIS109 4.9 43.0 1.0 O A:HIS91 5.0 38.1 1.0 C A:CYS86 5.0 37.8 1.0

Iron binding site 4 out of 36 in the Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Inhibitor MMV12 (MMV020670)


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 the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Inhibitor MMV12 (MMV020670) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe401 b:63.4 occ:1.00 N1 B:QKQ403 2.2 68.8 1.0 OD2 B:ASP323 2.2 69.2 1.0 NE2 B:HIS213 2.2 82.5 1.0 C8 B:QKQ403 2.4 70.9 1.0 NE2 B:HIS208 2.4 61.7 1.0 OD1 B:ASP323 2.6 75.3 1.0 CG B:ASP323 2.7 64.8 1.0 CD2 B:HIS213 3.0 82.3 1.0 C7 B:QKQ403 3.2 69.1 1.0 CE1 B:HIS208 3.3 61.7 1.0 CE1 B:HIS213 3.4 82.4 1.0 CD2 B:HIS208 3.5 62.5 1.0 C9 B:QKQ403 3.5 71.3 1.0 C6 B:QKQ403 4.1 70.8 1.0 CB B:ASP323 4.2 53.6 1.0 CG B:HIS213 4.2 83.4 1.0 C20 B:QKQ403 4.3 71.5 1.0 ND1 B:HIS213 4.4 82.7 1.0 C10 B:QKQ403 4.4 71.2 1.0 ND1 B:HIS208 4.4 62.6 1.0 CZ B:PHE319 4.6 71.1 1.0 CG B:HIS208 4.6 62.4 1.0 ND2 B:ASN202 4.7 42.4 1.0 OD1 B:ASN202 4.7 44.3 1.0 CA B:ASP323 4.9 48.8 1.0 CE1 B:PHE319 4.9 71.2 1.0 SG B:CYS209 4.9 82.0 1.0 CD1 B:LEU326 5.0 37.7 1.0

Iron binding site 5 out of 36 in the Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Inhibitor MMV12 (MMV020670)


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 the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Inhibitor MMV12 (MMV020670) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe402 b:44.6 occ:1.00 FE1 B:FES402 0.0 44.6 1.0 S1 B:FES402 2.2 38.7 1.0 S2 B:FES402 2.2 48.0 1.0 ND1 B:HIS109 2.2 57.1 1.0 ND1 B:HIS88 2.3 59.9 1.0 CG B:HIS109 3.0 59.0 1.0 CB B:HIS109 3.1 62.5 1.0 FE2 B:FES402 3.1 43.1 1.0 CG B:HIS88 3.2 56.4 1.0 CE1 B:HIS88 3.3 55.1 1.0 CE1 B:HIS109 3.3 57.3 1.0 CB B:HIS88 3.4 54.7 1.0 N B:HIS109 3.7 70.4 1.0 CA B:HIS109 4.0 68.4 1.0 CB B:TYR108 4.1 54.0 1.0 N B:ARG89 4.2 49.8 1.0 CD2 B:HIS109 4.2 59.2 1.0 SG B:CYS86 4.3 51.8 1.0 CD2 B:TYR108 4.3 52.1 1.0 NE2 B:HIS109 4.3 56.8 1.0 CD2 B:HIS88 4.4 56.4 1.0 NE2 B:HIS88 4.4 55.3 1.0 CG B:TYR108 4.4 53.2 1.0 SG B:CYS106 4.5 47.2 1.0 C B:TYR108 4.6 65.3 1.0 CB B:ARG89 4.6 49.9 1.0 CA B:HIS88 4.7 51.1 1.0 CD1 B:TRP111 4.8 51.6 1.0 C B:HIS88 4.8 52.1 1.0 C B:HIS109 4.8 67.7 1.0 NE1 B:TRP111 4.9 50.6 1.0 CA B:ARG89 4.9 49.1 1.0 CG B:TRP111 4.9 53.3 1.0 CA B:TYR108 4.9 58.9 1.0

Iron binding site 6 out of 36 in the Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Inhibitor MMV12 (MMV020670)


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 the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Inhibitor MMV12 (MMV020670) within 5.0Å range: probe atom residue distance (Å) B Occ B:Fe402 b:43.1 occ:1.00 FE2 B:FES402 0.0 43.1 1.0 S2 B:FES402 2.2 48.0 1.0 S1 B:FES402 2.2 38.7 1.0 SG B:CYS106 2.3 47.2 1.0 SG B:CYS86 2.4 51.8 1.0 CB B:CYS86 2.6 47.2 1.0 CB B:CYS106 2.8 53.6 1.0 FE1 B:FES402 3.1 44.6 1.0 CA B:CYS86 4.1 48.1 1.0 CA B:CYS106 4.3 55.9 1.0 CB B:TYR108 4.3 54.0 1.0 CB B:HIS91 4.3 43.0 1.0 CD2 B:LEU93 4.4 41.6 1.0 CB B:HIS88 4.6 54.7 1.0 N B:HIS109 4.6 70.4 1.0 O B:HIS91 4.7 41.3 1.0 N B:HIS91 4.8 39.7 1.0 C B:CYS86 4.8 47.6 1.0 C B:CYS106 4.8 56.0 1.0 N B:TYR108 4.8 56.0 1.0 N B:CYS86 4.9 48.7 1.0 CB B:TRP111 4.9 55.4 1.0 N B:ARG89 5.0 49.8 1.0 CA B:HIS91 5.0 40.7 1.0

Iron binding site 7 out of 36 in the Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Inhibitor MMV12 (MMV020670)


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 the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Inhibitor MMV12 (MMV020670) within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe401 b:64.3 occ:1.00 OD1 C:ASP323 2.3 80.0 1.0 N1 C:QKQ403 2.3 74.1 1.0 NE2 C:HIS213 2.3 80.2 1.0 NE2 C:HIS208 2.3 68.4 1.0 OD2 C:ASP323 2.3 72.9 1.0 CG C:ASP323 2.6 71.8 1.0 CD2 C:HIS213 2.8 84.1 1.0 C8 C:QKQ403 3.0 72.9 1.0 CE1 C:HIS208 3.0 67.8 1.0 C7 C:QKQ403 3.2 72.9 1.0 CD2 C:HIS208 3.5 67.7 1.0 CE1 C:HIS213 3.5 82.9 1.0 ND2 C:ASN202 4.0 47.2 1.0 CG C:HIS213 4.1 85.1 1.0 CB C:ASP323 4.1 63.6 1.0 C9 C:QKQ403 4.3 73.4 1.0 ND1 C:HIS208 4.3 68.5 1.0 ND1 C:HIS213 4.4 84.7 1.0 C6 C:QKQ403 4.4 72.2 1.0 CG C:HIS208 4.5 68.6 1.0 OD1 C:ASN202 4.5 46.4 1.0 CG C:ASN202 4.6 45.5 1.0 CZ C:PHE319 4.7 62.6 1.0 CA C:ASP323 4.8 58.4 1.0 SG C:CYS209 4.8 70.6 1.0 C20 C:QKQ403 4.8 72.9 1.0 CE1 C:PHE319 4.8 62.4 1.0 CD1 C:LEU326 5.0 39.4 1.0

Iron binding site 8 out of 36 in the Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Inhibitor MMV12 (MMV020670)


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 the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Inhibitor MMV12 (MMV020670) within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe402 b:61.6 occ:1.00 FE1 C:FES402 0.0 61.6 1.0 S2 C:FES402 2.2 53.2 1.0 S1 C:FES402 2.2 48.9 1.0 ND1 C:HIS88 2.2 73.6 1.0 ND1 C:HIS109 2.3 64.0 1.0 CG C:HIS109 3.1 66.4 1.0 FE2 C:FES402 3.1 49.3 1.0 CG C:HIS88 3.2 67.6 1.0 CE1 C:HIS88 3.2 69.0 1.0 CB C:HIS109 3.2 66.2 1.0 CE1 C:HIS109 3.3 65.1 1.0 CB C:HIS88 3.4 60.6 1.0 N C:HIS109 3.8 64.8 1.0 CA C:HIS109 4.1 66.0 1.0 N C:ARG89 4.1 53.6 1.0 CB C:TYR108 4.2 54.6 1.0 NE2 C:HIS88 4.3 69.5 1.0 CD2 C:HIS88 4.3 69.5 1.0 CD2 C:HIS109 4.3 67.3 1.0 CD2 C:TYR108 4.4 54.5 1.0 NE2 C:HIS109 4.4 65.4 1.0 SG C:CYS86 4.4 60.2 1.0 CB C:ARG89 4.4 55.7 1.0 SG C:CYS106 4.4 47.7 1.0 CG C:TYR108 4.6 53.6 1.0 CA C:HIS88 4.6 55.5 1.0 C C:TYR108 4.7 62.2 1.0 C C:HIS88 4.7 55.7 1.0 CA C:ARG89 4.8 52.9 1.0 CD1 C:TRP111 4.9 50.6 1.0 C C:HIS109 4.9 67.6 1.0 NE1 C:TRP111 4.9 51.2 1.0

Iron binding site 9 out of 36 in the Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Inhibitor MMV12 (MMV020670)


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 the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Inhibitor MMV12 (MMV020670) within 5.0Å range: probe atom residue distance (Å) B Occ C:Fe402 b:49.3 occ:1.00 FE2 C:FES402 0.0 49.3 1.0 S1 C:FES402 2.2 48.9 1.0 S2 C:FES402 2.2 53.2 1.0 SG C:CYS106 2.4 47.7 1.0 SG C:CYS86 2.4 60.2 1.0 CB C:CYS86 2.6 55.9 1.0 CB C:CYS106 3.0 51.9 1.0 FE1 C:FES402 3.1 61.6 1.0 CA C:CYS86 4.1 53.7 1.0 CB C:HIS88 4.3 60.6 1.0 CB C:HIS91 4.3 49.1 1.0 CA C:CYS106 4.4 52.3 1.0 C C:CYS86 4.6 52.9 1.0 N C:HIS91 4.7 48.5 1.0 CB C:TYR108 4.7 54.6 1.0 N C:ARG89 4.8 53.6 1.0 N C:HIS88 4.8 51.4 1.0 N C:HIS109 4.8 64.8 1.0 O C:HIS91 4.9 46.7 1.0 ND1 C:HIS88 4.9 73.6 1.0 O C:CYS86 4.9 53.1 1.0 CB C:TRP111 4.9 55.7 1.0 CD2 C:LEU93 4.9 45.4 1.0 N C:CYS86 5.0 52.7 1.0 C C:CYS106 5.0 48.9 1.0

Iron binding site 10 out of 36 in the Crystal Structure of the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Inhibitor MMV12 (MMV020670)


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 the Quaternary Ammonium Rieske Monooxygenase Cnta in Complex with Inhibitor MMV12 (MMV020670) within 5.0Å range: probe atom residue distance (Å) B Occ D:Fe401 b:63.5 occ:1.00 NE2 D:HIS213 2.3 74.5 1.0 OD2 D:ASP323 2.3 70.9 1.0 N1 D:QKQ403 2.3 68.8 1.0 NE2 D:HIS208 2.4 64.6 1.0 C8 D:QKQ403 2.4 69.9 1.0 OD1 D:ASP323 2.4 76.7 1.0 CG D:ASP323 2.7 67.4 1.0 CD2 D:HIS213 3.1 75.0 1.0 CE1 D:HIS208 3.2 64.3 1.0 CE1 D:HIS213 3.2 74.3 1.0 C7 D:QKQ403 3.4 68.5 1.0 CD2 D:HIS208 3.5 65.2 1.0 C9 D:QKQ403 3.6 70.9 1.0 ND2 D:ASN202 3.9 40.4 1.0 CB D:ASP323 4.2 56.5 1.0 CG D:HIS213 4.2 75.6 1.0 ND1 D:HIS213 4.2 75.0 1.0 ND1 D:HIS208 4.4 65.4 1.0 C6 D:QKQ403 4.4 68.7 1.0 C10 D:QKQ403 4.4 71.7 1.0 C20 D:QKQ403 4.5 70.5 1.0 OD1 D:ASN202 4.5 46.6 1.0 CG D:HIS208 4.6 65.1 1.0 CG D:ASN202 4.6 43.1 1.0 SG D:CYS209 4.6 87.8 1.0 CZ D:PHE319 4.8 68.8 1.0 CE1 D:PHE319 4.9 67.4 1.0 CA D:ASP323 4.9 49.9 1.0 O D:ASN202 4.9 36.0 1.0 CD1 D:LEU326 4.9 35.7 1.0

M.Quareshy, M.Shanmugam, E.Townsend, E.Jameson, T.D.H.Bugg, A.D.Cameron, Y.Chen. Structural Basis of Carnitine Monooxygenase Cnta Substrate Specificity, Inhibition and Inter-Subunit Electron Transfer. J.Biol.Chem. 2020.
ISSN: ESSN 1083-351X
PubMed: 33158989
DOI: 10.1074/JBC.RA120.016019