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Iron in PDB 1z01: 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction

Enzymatic activity of 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction

All present enzymatic activity of 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction:
1.14.13.61;

Protein crystallography data

The structure of 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction, PDB code: 1z01 was solved by B.M.Martins, T.Svetlitchnaia, H.Dobbek, 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 P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 104.460, 166.960, 173.460, 90.00, 90.00, 90.00
R / Rfree (%) 22 / 26

Iron Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 18;

Binding sites:

The binding sites of Iron atom in the 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction (pdb code 1z01). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 18 binding sites of Iron where determined in the 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction, PDB code: 1z01:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 18 in 1z01

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Iron binding site 1 out of 18 in the 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe501

b:25.5
occ:1.00
NE2 A:HIS225 2.1 22.2 1.0
OD2 A:ASP365 2.2 16.9 1.0
NE2 A:HIS221 2.2 22.3 1.0
O A:HOH1169 2.3 31.4 1.0
OD1 A:ASP365 2.5 23.2 1.0
CG A:ASP365 2.7 20.0 1.0
CE1 A:HIS225 3.0 21.2 1.0
CD2 A:HIS221 3.1 21.9 1.0
CD2 A:HIS225 3.1 23.6 1.0
CE1 A:HIS221 3.3 22.0 1.0
ND1 A:HIS225 4.1 20.8 1.0
CB A:ASP365 4.1 18.9 1.0
O A:HOH1058 4.2 45.5 1.0
OD1 A:ASN215 4.2 23.1 1.0
CG A:HIS225 4.2 22.6 1.0
CE2 A:PHE361 4.3 22.5 1.0
CG A:HIS221 4.3 23.3 1.0
ND1 A:HIS221 4.4 22.8 1.0
O A:HOH581 4.4 28.4 1.0
O A:HOH1153 4.5 49.7 1.0
CZ A:PHE361 4.7 22.2 1.0
CA A:ASP365 5.0 18.5 1.0
CG A:ASN215 5.0 20.2 1.0
ND2 A:ASN215 5.0 19.3 1.0

Iron binding site 2 out of 18 in 1z01

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Iron binding site 2 out of 18 in the 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:13.3
occ:1.00
FE1 A:FES500 0.0 13.3 1.0
ND1 A:HIS86 2.2 8.3 1.0
ND1 A:HIS108 2.2 13.7 1.0
S1 A:FES500 2.2 13.5 1.0
S2 A:FES500 2.3 13.6 1.0
FE2 A:FES500 2.6 13.6 1.0
CG A:HIS108 3.0 14.0 1.0
CG A:HIS86 3.1 10.5 1.0
CE1 A:HIS86 3.2 10.3 1.0
CB A:HIS108 3.2 15.2 1.0
CE1 A:HIS108 3.2 14.7 1.0
CB A:HIS86 3.3 9.9 1.0
N A:HIS108 3.9 14.4 1.0
CA A:HIS108 4.1 15.5 1.0
N A:ARG87 4.2 12.6 1.0
CD2 A:HIS108 4.2 14.6 1.0
CD2 A:HIS86 4.2 9.1 1.0
NE2 A:HIS108 4.3 15.5 1.0
NE2 A:HIS86 4.3 10.0 1.0
CB A:TYR107 4.4 14.8 1.0
SG A:CYS84 4.4 12.4 1.0
CB A:ARG87 4.4 14.3 1.0
SG A:CYS105 4.5 13.5 1.0
CG A:ARG87 4.6 13.9 1.0
CD1 A:PHE110 4.6 12.6 1.0
CA A:HIS86 4.6 12.5 1.0
CG A:TYR107 4.7 16.2 1.0
C A:HIS86 4.8 12.3 1.0
C A:TYR107 4.8 14.9 1.0
CE1 A:PHE110 4.8 11.8 1.0
CD1 A:TYR107 4.9 17.5 1.0
C A:HIS108 4.9 16.2 1.0
CA A:ARG87 4.9 13.3 1.0

Iron binding site 3 out of 18 in 1z01

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Iron binding site 3 out of 18 in the 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe500

b:13.6
occ:1.00
FE2 A:FES500 0.0 13.6 1.0
S2 A:FES500 2.2 13.6 1.0
S1 A:FES500 2.2 13.5 1.0
SG A:CYS105 2.3 13.5 1.0
SG A:CYS84 2.4 12.4 1.0
FE1 A:FES500 2.6 13.3 1.0
CB A:CYS84 3.1 11.5 1.0
CB A:CYS105 3.2 14.2 1.0
CB A:HIS86 3.9 9.9 1.0
CG2 A:VAL89 4.1 13.2 1.0
CB A:TYR107 4.3 14.8 1.0
ND1 A:HIS86 4.4 8.3 1.0
ND1 A:HIS108 4.4 13.7 1.0
N A:HIS108 4.4 14.4 1.0
N A:ARG87 4.5 12.6 1.0
CB A:PHE110 4.6 15.1 1.0
CA A:CYS84 4.6 11.7 1.0
CG A:HIS86 4.6 10.5 1.0
CA A:CYS105 4.7 15.5 1.0
CG A:PHE110 4.9 13.7 1.0
N A:HIS86 4.9 11.7 1.0
CA A:HIS86 4.9 12.5 1.0
CB A:HIS108 5.0 15.2 1.0
CD1 A:PHE110 5.0 12.6 1.0

Iron binding site 4 out of 18 in 1z01

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Iron binding site 4 out of 18 in the 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe501

b:19.2
occ:1.00
OD2 B:ASP365 2.1 18.8 1.0
NE2 B:HIS225 2.2 20.8 1.0
NE2 B:HIS221 2.2 21.4 1.0
OD1 B:ASP365 2.5 21.4 1.0
O B:HOH1121 2.6 24.1 1.0
CG B:ASP365 2.6 19.0 1.0
CE1 B:HIS225 3.1 20.5 1.0
CD2 B:HIS221 3.1 21.6 1.0
CE1 B:HIS221 3.3 20.6 1.0
CD2 B:HIS225 3.3 22.4 1.0
O B:HOH860 3.4 51.6 1.0
CB B:ASP365 4.1 18.8 1.0
OD1 B:ASN215 4.1 22.3 1.0
ND1 B:HIS225 4.2 20.4 1.0
CE2 B:PHE361 4.3 19.4 1.0
CG B:HIS221 4.3 22.8 1.0
ND1 B:HIS221 4.3 21.3 1.0
CG B:HIS225 4.4 22.0 1.0
O B:HOH655 4.4 25.5 1.0
O B:HOH1075 4.6 52.7 1.0
CZ B:PHE361 4.8 18.9 1.0
CA B:ASP365 4.9 18.4 1.0
CG B:ASN215 4.9 19.6 1.0
ND2 B:ASN215 5.0 17.0 1.0
O B:HOH992 5.0 32.1 1.0

Iron binding site 5 out of 18 in 1z01

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Iron binding site 5 out of 18 in the 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe500

b:16.4
occ:1.00
FE1 B:FES500 0.0 16.4 1.0
ND1 B:HIS86 2.2 9.9 1.0
ND1 B:HIS108 2.2 13.4 1.0
S1 B:FES500 2.2 15.3 1.0
S2 B:FES500 2.2 16.1 1.0
FE2 B:FES500 2.6 17.7 1.0
CG B:HIS108 3.0 14.2 1.0
CG B:HIS86 3.2 10.7 1.0
CE1 B:HIS86 3.2 11.9 1.0
CB B:HIS108 3.2 14.8 1.0
CE1 B:HIS108 3.3 15.1 1.0
CB B:HIS86 3.4 11.1 1.0
N B:HIS108 3.7 18.1 1.0
CA B:HIS108 4.0 17.1 1.0
CD2 B:HIS108 4.2 13.7 1.0
CB B:TYR107 4.2 17.3 1.0
N B:ARG87 4.3 13.7 1.0
NE2 B:HIS86 4.3 11.7 1.0
NE2 B:HIS108 4.3 15.1 1.0
CD2 B:HIS86 4.3 11.3 1.0
SG B:CYS84 4.4 15.2 1.0
CB B:ARG87 4.5 15.1 1.0
CG B:ARG87 4.5 16.2 1.0
SG B:CYS105 4.6 14.4 1.0
CG B:TYR107 4.6 17.7 1.0
CD1 B:PHE110 4.6 14.6 1.0
C B:TYR107 4.7 18.1 1.0
CA B:HIS86 4.7 12.6 1.0
C B:HIS108 4.8 17.4 1.0
CE1 B:PHE110 4.8 14.4 1.0
CD1 B:TYR107 4.9 19.6 1.0
C B:HIS86 4.9 13.3 1.0

Iron binding site 6 out of 18 in 1z01

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Iron binding site 6 out of 18 in the 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe500

b:17.7
occ:1.00
FE2 B:FES500 0.0 17.7 1.0
S1 B:FES500 2.2 15.3 1.0
S2 B:FES500 2.2 16.1 1.0
SG B:CYS84 2.4 15.2 1.0
SG B:CYS105 2.4 14.4 1.0
FE1 B:FES500 2.6 16.4 1.0
CB B:CYS105 3.1 16.0 1.0
CB B:CYS84 3.2 14.9 1.0
CB B:HIS86 4.0 11.1 1.0
CG2 B:VAL89 4.1 11.7 1.0
CB B:TYR107 4.2 17.3 1.0
N B:HIS108 4.3 18.1 1.0
ND1 B:HIS86 4.4 9.9 1.0
ND1 B:HIS108 4.5 13.4 1.0
CA B:CYS105 4.6 16.7 1.0
CB B:PHE110 4.6 15.7 1.0
CA B:CYS84 4.6 12.7 1.0
N B:ARG87 4.6 13.7 1.0
CG B:HIS86 4.7 10.7 1.0
CG B:PHE110 4.9 15.2 1.0
N B:PHE110 4.9 14.5 1.0
CD1 B:PHE110 5.0 14.6 1.0
N B:HIS86 5.0 11.3 1.0
N B:TYR107 5.0 17.0 1.0
CB B:HIS108 5.0 14.8 1.0

Iron binding site 7 out of 18 in 1z01

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Iron binding site 7 out of 18 in the 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe501

b:25.3
occ:1.00
OD2 C:ASP365 2.1 21.9 1.0
NE2 C:HIS225 2.2 21.4 1.0
NE2 C:HIS221 2.3 24.0 1.0
O C:HOH1104 2.4 29.1 1.0
OD1 C:ASP365 2.4 23.6 1.0
CG C:ASP365 2.6 21.8 1.0
CE1 C:HIS225 3.0 20.1 1.0
CD2 C:HIS221 3.2 24.7 1.0
CD2 C:HIS225 3.3 21.9 1.0
CE1 C:HIS221 3.4 24.1 1.0
CB C:ASP365 4.1 18.9 1.0
OD1 C:ASN215 4.1 25.0 1.0
ND1 C:HIS225 4.2 19.8 1.0
CE2 C:PHE361 4.3 19.7 1.0
CG C:HIS225 4.3 22.0 1.0
CG C:HIS221 4.4 25.4 1.0
O C:HOH626 4.4 24.8 1.0
ND1 C:HIS221 4.4 24.6 1.0
O C:HOH670 4.6 34.4 1.0
CZ C:PHE361 4.7 20.2 1.0
CA C:ASP365 4.9 18.3 1.0
CG C:ASN215 4.9 22.1 1.0
ND2 C:ASN215 5.0 21.6 1.0

Iron binding site 8 out of 18 in 1z01

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Iron binding site 8 out of 18 in the 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe500

b:15.5
occ:1.00
FE1 C:FES500 0.0 15.5 1.0
S1 C:FES500 2.2 15.7 1.0
ND1 C:HIS108 2.2 12.5 1.0
S2 C:FES500 2.2 14.3 1.0
ND1 C:HIS86 2.3 9.0 1.0
FE2 C:FES500 2.6 14.5 1.0
CG C:HIS108 3.0 13.6 1.0
CB C:HIS108 3.2 14.8 1.0
CG C:HIS86 3.2 8.8 1.0
CE1 C:HIS108 3.2 13.2 1.0
CE1 C:HIS86 3.3 9.8 1.0
CB C:HIS86 3.5 10.7 1.0
N C:HIS108 3.7 15.5 1.0
CA C:HIS108 4.0 16.1 1.0
CD2 C:HIS108 4.2 14.3 1.0
CB C:TYR107 4.2 14.8 1.0
N C:ARG87 4.3 11.7 1.0
NE2 C:HIS108 4.3 12.3 1.0
SG C:CYS84 4.3 14.6 1.0
NE2 C:HIS86 4.4 8.3 1.0
CD2 C:HIS86 4.4 8.9 1.0
SG C:CYS105 4.5 13.3 1.0
CB C:ARG87 4.6 11.7 1.0
CG C:ARG87 4.6 13.2 1.0
CG C:TYR107 4.6 14.5 1.0
C C:TYR107 4.6 15.6 1.0
CD1 C:PHE110 4.8 13.2 1.0
C C:HIS108 4.8 16.9 1.0
CD1 C:TYR107 4.8 16.9 1.0
CA C:HIS86 4.8 11.4 1.0
C C:HIS86 4.9 13.3 1.0
CE1 C:PHE110 5.0 14.0 1.0

Iron binding site 9 out of 18 in 1z01

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Iron binding site 9 out of 18 in the 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction within 5.0Å range:
probe atom residue distance (Å) B Occ
C:Fe500

b:14.5
occ:1.00
FE2 C:FES500 0.0 14.5 1.0
S1 C:FES500 2.2 15.7 1.0
S2 C:FES500 2.2 14.3 1.0
SG C:CYS84 2.3 14.6 1.0
SG C:CYS105 2.4 13.3 1.0
FE1 C:FES500 2.6 15.5 1.0
CB C:CYS105 3.1 16.2 1.0
CB C:CYS84 3.2 13.4 1.0
CG2 C:VAL89 4.0 14.5 1.0
CB C:HIS86 4.0 10.7 1.0
CB C:TYR107 4.2 14.8 1.0
N C:HIS108 4.3 15.5 1.0
ND1 C:HIS86 4.4 9.0 1.0
ND1 C:HIS108 4.5 12.5 1.0
CA C:CYS105 4.6 17.3 1.0
CA C:CYS84 4.6 12.5 1.0
N C:ARG87 4.7 11.7 1.0
CB C:PHE110 4.7 15.2 1.0
CG C:HIS86 4.7 8.8 1.0
CB C:HIS108 4.9 14.8 1.0
N C:TYR107 4.9 15.2 1.0
CG C:PHE110 5.0 13.3 1.0
N C:PHE110 5.0 15.5 1.0

Iron binding site 10 out of 18 in 1z01

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Iron binding site 10 out of 18 in the 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of 2-Oxoquinoline 8-Monooxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe501

b:22.0
occ:1.00
NE2 D:HIS225 2.1 22.3 1.0
OD2 D:ASP365 2.2 17.9 1.0
NE2 D:HIS221 2.2 21.6 1.0
OD1 D:ASP365 2.5 23.5 1.0
O D:HOH1164 2.6 31.5 1.0
CG D:ASP365 2.6 20.7 1.0
CD2 D:HIS221 3.0 22.7 1.0
CE1 D:HIS225 3.0 21.5 1.0
CD2 D:HIS225 3.2 21.4 1.0
CE1 D:HIS221 3.3 22.3 1.0
O D:HOH1069 3.3 55.2 1.0
OD1 D:ASN215 4.1 21.7 1.0
CB D:ASP365 4.1 18.9 1.0
ND1 D:HIS225 4.2 22.3 1.0
CG D:HIS221 4.2 24.1 1.0
CG D:HIS225 4.3 22.5 1.0
ND1 D:HIS221 4.3 24.0 1.0
CE2 D:PHE361 4.4 19.2 1.0
O D:HOH852 4.6 34.4 1.0
O D:HOH561 4.6 27.9 1.0
CZ D:PHE361 4.8 20.0 1.0
ND2 D:ASN215 4.9 19.3 1.0
CG D:ASN215 4.9 20.3 1.0
CA D:ASP365 5.0 18.4 1.0

Reference:

B.M.Martins, T.Svetlitchnaia, H.Dobbek. 2-Oxoquinoline 8-Monooxygenase Oxygenase Component: Active Site Modulation By Rieske-[2FE-2S] Center Oxidation/Reduction Structure V. 13 817 2005.
ISSN: ISSN 0969-2126
PubMed: 15893671
DOI: 10.1016/J.STR.2005.03.008
Page generated: Sun Dec 13 14:38:33 2020

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