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Iron in PDB 1z02: 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: 1z02 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 (°) 102.030, 169.970, 175.350, 90.00, 90.00, 90.00
R / Rfree (%) 20 / 24

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 1z02). 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: 1z02:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 18 in 1z02

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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:14.8
occ:1.00
 NE2 A:HIS225 2.0 13.7 1.0
NE2 A:HIS221 2.2 17.8 1.0
OD2 A:ASP365 2.2 11.2 1.0
O A:HOH1295 2.3 31.3 1.0
O A:HOH1296 2.3 20.6 1.0
OD1 A:ASP365 2.5 11.2 1.0
CG A:ASP365 2.6 10.7 1.0
CE1 A:HIS225 2.9 12.8 1.0
CD2 A:HIS221 3.1 18.5 1.0
CD2 A:HIS225 3.1 13.5 1.0
CE1 A:HIS221 3.2 18.5 1.0
ND1 A:HIS225 4.0 13.0 1.0
CB A:ASP365 4.1 10.8 1.0
CG A:HIS225 4.2 15.5 1.0
CG A:HIS221 4.3 20.2 1.0
ND1 A:HIS221 4.3 19.3 1.0
ND2 A:ASN215 4.4 10.5 1.0
O A:HOH1119 4.6 43.1 1.0
CE2 A:PHE361 4.6 15.0 1.0
OD1 A:ASN215 4.7 8.6 1.0
O A:ASN215 4.8 14.2 1.0
O A:HOH1147 4.8 44.5 1.0
CG1 A:VAL224 4.8 9.4 1.0
ND2 A:ASN362 4.9 15.9 1.0
CA A:ASP365 4.9 11.8 1.0
CG A:ASN215 4.9 10.5 1.0

Iron binding site 2 out of 18 in 1z02

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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:12.9
occ:1.00
 FE1 A:FES500 0.0 12.9 1.0
S1 A:FES500 2.2 12.6 1.0
S2 A:FES500 2.3 15.3 1.0
ND1 A:HIS86 2.4 8.9 1.0
ND1 A:HIS108 2.4 13.5 1.0
FE2 A:FES500 2.6 10.3 1.0
CG A:HIS108 3.2 13.6 1.0
CG A:HIS86 3.2 10.1 1.0
CB A:HIS108 3.3 14.7 1.0
CB A:HIS86 3.3 11.2 1.0
CE1 A:HIS86 3.4 9.3 1.0
CE1 A:HIS108 3.5 13.2 1.0
N A:HIS108 3.7 15.1 1.0
CB A:TYR107 4.1 11.2 1.0
CA A:HIS108 4.1 15.0 1.0
CD1 A:TYR107 4.3 17.4 1.0
CG A:TYR107 4.4 14.9 1.0
CD2 A:HIS108 4.4 13.9 1.0
CD2 A:HIS86 4.4 8.7 1.0
N A:ARG87 4.4 10.5 1.0
SG A:CYS84 4.5 11.0 1.0
NE2 A:HIS86 4.5 9.4 1.0
NE2 A:HIS108 4.5 14.0 1.0
CD1 A:PHE110 4.5 6.8 1.0
SG A:CYS105 4.6 10.9 1.0
CG A:ARG87 4.6 14.4 1.0
C A:TYR107 4.7 12.9 1.0
CA A:HIS86 4.7 9.7 1.0
CB A:ARG87 4.8 11.0 1.0
O B:HOH704 4.8 19.4 1.0
CE1 A:PHE110 4.8 6.7 1.0
C A:HIS108 4.9 16.3 1.0
CA A:TYR107 5.0 11.9 1.0
C A:HIS86 5.0 8.9 1.0

Iron binding site 3 out of 18 in 1z02

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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:10.3
occ:1.00
 FE2 A:FES500 0.0 10.3 1.0
S1 A:FES500 2.2 12.6 1.0
S2 A:FES500 2.2 15.3 1.0
SG A:CYS105 2.3 10.9 1.0
SG A:CYS84 2.4 11.0 1.0
FE1 A:FES500 2.6 12.9 1.0
CB A:CYS105 3.1 9.5 1.0
CB A:CYS84 3.2 7.1 1.0
CB A:HIS86 4.0 11.2 1.0
CB A:TYR107 4.2 11.2 1.0
N A:HIS108 4.4 15.1 1.0
CB A:PHE110 4.5 8.6 1.0
ND1 A:HIS86 4.6 8.9 1.0
CA A:CYS105 4.6 10.1 1.0
N A:ARG87 4.6 10.5 1.0
CB A:VAL89 4.6 10.7 1.0
CA A:CYS84 4.7 6.9 1.0
CG A:HIS86 4.8 10.1 1.0
ND1 A:HIS108 4.8 13.5 1.0
CG A:PHE110 4.8 7.8 1.0
N A:TYR107 4.8 9.8 1.0
N A:PHE110 4.9 9.0 1.0
CG2 A:VAL89 4.9 11.9 1.0
CD1 A:PHE110 5.0 6.8 1.0
N A:HIS86 5.0 10.8 1.0
CA A:HIS86 5.0 9.7 1.0
CA A:TYR107 5.0 11.9 1.0

Iron binding site 4 out of 18 in 1z02

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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:13.1
occ:1.00
 NE2 B:HIS225 2.1 12.8 1.0
OD2 B:ASP365 2.2 10.4 1.0
NE2 B:HIS221 2.2 15.6 1.0
O B:HOH1390 2.3 27.6 1.0
O B:HOH1391 2.4 10.3 1.0
OD1 B:ASP365 2.5 13.4 1.0
CG B:ASP365 2.7 10.0 1.0
CE1 B:HIS225 3.0 10.2 1.0
CD2 B:HIS221 3.2 15.5 1.0
CD2 B:HIS225 3.2 11.2 1.0
CE1 B:HIS221 3.2 14.9 1.0
CB B:ASP365 4.2 11.1 1.0
ND1 B:HIS225 4.2 14.7 1.0
CG B:HIS225 4.3 13.7 1.0
CG B:HIS221 4.3 18.1 1.0
ND1 B:HIS221 4.3 16.1 1.0
O B:HOH1140 4.5 33.2 1.0
ND2 B:ASN215 4.5 9.2 1.0
CE2 B:PHE361 4.5 12.8 1.0
O B:HOH619 4.5 22.4 1.0
OD1 B:ASN215 4.6 9.6 1.0
O B:ASN215 4.7 13.7 1.0
ND2 B:ASN362 4.7 9.2 1.0
CA B:ASP365 4.9 11.2 1.0
CZ B:PHE361 4.9 12.7 1.0
CG1 B:VAL224 4.9 10.4 1.0
CG B:ASN215 4.9 11.3 1.0

Iron binding site 5 out of 18 in 1z02

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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:16.0
occ:1.00
 FE1 B:FES500 0.0 16.0 1.0
S1 B:FES500 2.2 12.4 1.0
S2 B:FES500 2.2 17.7 1.0
ND1 B:HIS86 2.3 11.0 1.0
ND1 B:HIS108 2.4 14.4 1.0
FE2 B:FES500 2.6 18.9 1.0
CG B:HIS108 3.2 16.4 1.0
CG B:HIS86 3.2 10.1 1.0
CB B:HIS108 3.3 15.0 1.0
CB B:HIS86 3.4 9.9 1.0
CE1 B:HIS86 3.4 7.5 1.0
CE1 B:HIS108 3.4 15.1 1.0
N B:HIS108 3.7 16.1 1.0
CA B:HIS108 4.1 17.0 1.0
CB B:TYR107 4.1 17.0 1.0
N B:ARG87 4.4 10.0 1.0
CD2 B:HIS108 4.4 17.1 1.0
CD1 B:TYR107 4.4 18.4 1.0
CD2 B:HIS86 4.4 9.9 1.0
CG B:TYR107 4.4 17.6 1.0
NE2 B:HIS86 4.5 10.2 1.0
NE2 B:HIS108 4.5 16.3 1.0
O B:HOH783 4.5 28.2 1.0
CD1 B:PHE110 4.5 12.3 1.0
SG B:CYS84 4.5 12.3 1.0
SG B:CYS105 4.6 12.1 1.0
CG B:ARG87 4.7 15.0 1.0
CB B:ARG87 4.7 11.4 1.0
C B:TYR107 4.7 15.7 1.0
CA B:HIS86 4.8 11.0 1.0
CE1 B:PHE110 4.8 12.8 1.0
C B:HIS108 4.9 17.5 1.0
C B:HIS86 5.0 10.9 1.0

Iron binding site 6 out of 18 in 1z02

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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:18.9
occ:1.00
 FE2 B:FES500 0.0 18.9 1.0
S2 B:FES500 2.2 17.7 1.0
S1 B:FES500 2.2 12.4 1.0
SG B:CYS105 2.4 12.1 1.0
SG B:CYS84 2.5 12.3 1.0
FE1 B:FES500 2.6 16.0 1.0
CB B:CYS105 3.1 12.9 1.0
CB B:CYS84 3.2 9.8 1.0
CG2 B:VAL89 3.9 16.8 1.0
CB B:HIS86 3.9 9.9 1.0
CB B:TYR107 4.3 17.0 1.0
N B:HIS108 4.4 16.1 1.0
CB B:PHE110 4.5 12.6 1.0
ND1 B:HIS86 4.5 11.0 1.0
CA B:CYS105 4.6 13.4 1.0
N B:ARG87 4.6 10.0 1.0
CA B:CYS84 4.7 8.7 1.0
CG B:HIS86 4.7 10.1 1.0
CG B:PHE110 4.8 12.2 1.0
ND1 B:HIS108 4.8 14.4 1.0
CD1 B:PHE110 4.9 12.3 1.0
N B:HIS86 4.9 9.1 1.0
CA B:HIS86 4.9 11.0 1.0
N B:PHE110 4.9 11.6 1.0
N B:TYR107 5.0 13.2 1.0

Iron binding site 7 out of 18 in 1z02

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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:16.9
occ:1.00
 NE2 C:HIS225 2.1 16.5 1.0
OD2 C:ASP365 2.2 10.4 1.0
NE2 C:HIS221 2.2 14.0 1.0
O C:HOH1341 2.3 29.5 1.0
O C:HOH1342 2.4 17.7 1.0
OD1 C:ASP365 2.5 10.7 1.0
CG C:ASP365 2.6 8.8 1.0
CE1 C:HIS225 3.0 15.4 1.0
CD2 C:HIS221 3.1 12.3 1.0
CD2 C:HIS225 3.2 15.4 1.0
CE1 C:HIS221 3.2 14.3 1.0
CB C:ASP365 4.1 9.7 1.0
ND1 C:HIS225 4.2 14.5 1.0
CG C:HIS225 4.3 17.3 1.0
CG C:HIS221 4.3 16.8 1.0
ND1 C:HIS221 4.3 14.5 1.0
ND2 C:ASN215 4.4 8.8 1.0
CE2 C:PHE361 4.5 14.1 1.0
O C:HOH675 4.5 30.6 1.0
O C:HOH742 4.6 26.4 1.0
OD1 C:ASN215 4.7 15.1 1.0
ND2 C:ASN362 4.7 13.8 1.0
O C:ASN215 4.8 9.3 1.0
CG1 C:VAL224 4.8 17.5 1.0
CA C:ASP365 4.9 10.6 1.0
CG C:ASN215 4.9 11.3 1.0
CZ C:PHE361 4.9 13.2 1.0

Iron binding site 8 out of 18 in 1z02

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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:12.7
occ:1.00
 FE1 C:FES500 0.0 12.7 1.0
S1 C:FES500 2.2 13.2 1.0
ND1 C:HIS108 2.3 12.4 1.0
S2 C:FES500 2.3 14.3 1.0
ND1 C:HIS86 2.4 8.3 1.0
FE2 C:FES500 2.7 17.8 1.0
CG C:HIS108 3.2 12.7 1.0
CG C:HIS86 3.2 7.8 1.0
CE1 C:HIS108 3.3 10.5 1.0
CB C:HIS108 3.3 14.4 1.0
CE1 C:HIS86 3.4 9.0 1.0
CB C:HIS86 3.4 9.8 1.0
N C:HIS108 3.8 16.0 1.0
CB C:TYR107 4.1 15.0 1.0
CA C:HIS108 4.1 14.9 1.0
CD1 C:TYR107 4.2 17.9 1.0
CG C:TYR107 4.3 15.2 1.0
CD2 C:HIS108 4.4 13.9 1.0
NE2 C:HIS108 4.4 13.5 1.0
CD2 C:HIS86 4.4 8.5 1.0
NE2 C:HIS86 4.5 10.0 1.0
N C:ARG87 4.5 11.9 1.0
SG C:CYS84 4.5 13.0 1.0
CD1 C:PHE110 4.6 12.8 1.0
SG C:CYS105 4.7 10.9 1.0
CG C:ARG87 4.7 12.4 1.0
C C:TYR107 4.7 14.1 1.0
CA C:HIS86 4.8 11.4 1.0
CB C:ARG87 4.8 12.0 1.0
O A:HOH740 4.8 30.9 1.0
CE1 C:PHE110 4.8 13.8 1.0

Iron binding site 9 out of 18 in 1z02

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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:17.8
occ:1.00
 FE2 C:FES500 0.0 17.8 1.0
S2 C:FES500 2.2 14.3 1.0
S1 C:FES500 2.2 13.2 1.0
SG C:CYS84 2.4 13.0 1.0
SG C:CYS105 2.5 10.9 1.0
FE1 C:FES500 2.7 12.7 1.0
CB C:CYS105 3.2 12.1 1.0
CB C:CYS84 3.3 13.6 1.0
CB C:HIS86 4.0 9.8 1.0
CB C:TYR107 4.3 15.0 1.0
N C:HIS108 4.5 16.0 1.0
CB C:PHE110 4.5 12.3 1.0
ND1 C:HIS86 4.5 8.3 1.0
CB C:VAL89 4.5 14.2 1.0
CA C:CYS105 4.6 11.9 1.0
N C:ARG87 4.6 11.9 1.0
CG2 C:VAL89 4.7 15.6 1.0
CA C:CYS84 4.7 12.6 1.0
CG C:HIS86 4.8 7.8 1.0
ND1 C:HIS108 4.8 12.4 1.0
CG C:PHE110 4.8 12.6 1.0
N C:TYR107 4.9 12.8 1.0
CD1 C:PHE110 4.9 12.8 1.0
N C:PHE110 5.0 12.8 1.0
N C:HIS86 5.0 10.9 1.0

Iron binding site 10 out of 18 in 1z02

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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:16.4
occ:1.00
 OD2 D:ASP365 2.2 12.8 1.0
NE2 D:HIS225 2.2 14.3 1.0
O D:HOH1317 2.2 25.0 1.0
NE2 D:HIS221 2.2 17.2 1.0
O D:HOH1318 2.3 15.3 1.0
OD1 D:ASP365 2.4 16.2 1.0
CG D:ASP365 2.6 13.2 1.0
CE1 D:HIS225 3.0 14.1 1.0
CD2 D:HIS221 3.2 19.7 1.0
CD2 D:HIS225 3.3 13.4 1.0
CE1 D:HIS221 3.3 17.4 1.0
CB D:ASP365 4.1 10.2 1.0
ND1 D:HIS225 4.2 16.2 1.0
CG D:HIS225 4.3 15.9 1.0
ND2 D:ASN215 4.3 11.6 1.0
CG D:HIS221 4.3 21.1 1.0
ND1 D:HIS221 4.3 20.7 1.0
CE2 D:PHE361 4.5 14.1 1.0
O D:HOH633 4.6 20.9 1.0
O D:ASN215 4.6 11.0 1.0
OD1 D:ASN215 4.6 10.9 1.0
O D:HOH732 4.6 28.4 1.0
ND2 D:ASN362 4.8 16.9 1.0
CG D:ASN215 4.9 10.5 1.0
CA D:ASP365 4.9 12.0 1.0
O D:HOH823 4.9 23.7 1.0
CG1 D:VAL224 4.9 17.1 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: Sat Aug 3 18:09:20 2024

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