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Iron in PDB 2b76: E. Coli Quinol Fumarate Reductase Frda E49Q Mutation

Enzymatic activity of E. Coli Quinol Fumarate Reductase Frda E49Q Mutation

All present enzymatic activity of E. Coli Quinol Fumarate Reductase Frda E49Q Mutation:
1.3.99.1;

Protein crystallography data

The structure of E. Coli Quinol Fumarate Reductase Frda E49Q Mutation, PDB code: 2b76 was solved by E.Maklashina, T.M.Iverson, Y.Sher, V.Kotlyar, O.Mirza, J.Andrell, J.M.Hudson, F.A.Armstrong, G.Cecchini, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 3.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 96.802, 139.527, 273.972, 90.00, 90.00, 90.00
R / Rfree (%) 24.8 / 28.4

Iron Binding Sites:

Pages:

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

Binding sites:

The binding sites of Iron atom in the E. Coli Quinol Fumarate Reductase Frda E49Q Mutation (pdb code 2b76). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 18 binding sites of Iron where determined in the E. Coli Quinol Fumarate Reductase Frda E49Q Mutation, PDB code: 2b76:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Iron binding site 1 out of 18 in 2b76

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Iron binding site 1 out of 18 in the E. Coli Quinol Fumarate Reductase Frda E49Q Mutation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 1 of E. Coli Quinol Fumarate Reductase Frda E49Q Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe244

b:4.0
occ:1.00
 FE1 B:FES244 0.0 4.0 1.0
S1 B:FES244 2.2 1.0 1.0
S2 B:FES244 2.3 6.0 1.0
CB B:CYS77 2.3 15.8 1.0
SG B:CYS65 2.3 17.9 1.0
SG B:CYS77 2.5 17.9 1.0
FE2 B:FES244 2.6 9.0 1.0
CA B:CYS77 3.5 15.8 1.0
CB B:CYS65 3.6 16.3 1.0
N B:ALA60 4.1 11.4 1.0
SG B:CYS57 4.1 9.2 1.0
CA B:ALA60 4.2 9.9 1.0
N B:CYS77 4.2 14.6 1.0
N B:CYS65 4.3 16.2 1.0
SG B:CYS62 4.5 18.2 1.0
CA B:CYS65 4.5 16.4 1.0
C B:CYS77 4.6 16.5 1.0
CB B:LEU75 4.6 9.5 1.0
CD1 B:LEU75 4.7 9.2 1.0
N B:ARG58 4.7 9.2 1.0
CD2 B:LEU37 4.7 9.2 1.0
N B:MET59 4.9 13.4 1.0
CA B:ARG58 4.9 9.2 1.0

Iron binding site 2 out of 18 in 2b76

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Iron binding site 2 out of 18 in the E. Coli Quinol Fumarate Reductase Frda E49Q Mutation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 2 of E. Coli Quinol Fumarate Reductase Frda E49Q Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe244

b:9.0
occ:1.00
 FE2 B:FES244 0.0 9.0 1.0
SG B:CYS62 2.0 18.2 1.0
S2 B:FES244 2.2 6.0 1.0
SG B:CYS57 2.2 9.2 1.0
S1 B:FES244 2.2 1.0 1.0
FE1 B:FES244 2.6 4.0 1.0
CB B:CYS57 3.4 9.2 1.0
CB B:CYS62 3.4 17.3 1.0
N B:CYS62 3.5 17.8 1.0
N B:CYS57 3.5 9.2 1.0
N B:GLY63 3.7 15.8 1.0
CA B:CYS62 3.9 17.3 1.0
N B:ARG58 3.9 9.2 1.0
CA B:CYS57 3.9 9.2 1.0
N B:ILE61 4.2 12.5 1.0
C B:CYS62 4.2 17.2 1.0
N B:SER64 4.3 16.9 1.0
SG B:CYS77 4.3 17.9 1.0
C B:CYS57 4.4 9.2 1.0
N B:ALA60 4.4 11.4 1.0
N B:SER56 4.5 9.2 1.0
C B:SER56 4.6 9.2 1.0
SG B:CYS65 4.6 17.9 1.0
C B:ILE61 4.6 17.7 1.0
CA B:ALA60 4.6 9.9 1.0
N B:MET59 4.6 13.4 1.0
CA B:GLY63 4.8 16.8 1.0
CA B:ARG58 4.8 9.2 1.0
CB B:CYS77 4.8 15.8 1.0
C B:ALA60 4.8 10.3 1.0
N B:CYS65 4.9 16.2 1.0
CA B:ILE61 5.0 15.4 1.0
CA B:SER56 5.0 9.2 1.0
C B:GLY63 5.0 16.2 1.0

Iron binding site 3 out of 18 in 2b76

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Iron binding site 3 out of 18 in the E. Coli Quinol Fumarate Reductase Frda E49Q Mutation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 3 of E. Coli Quinol Fumarate Reductase Frda E49Q Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe245

b:24.5
occ:1.00
 FE1 B:F3S245 0.0 24.5 1.0
SG B:CYS204 2.2 24.1 1.0
S3 B:F3S245 2.2 11.6 1.0
S1 B:F3S245 2.3 15.1 1.0
S2 B:F3S245 2.3 11.5 1.0
FE3 B:F3S245 2.6 13.1 1.0
FE4 B:F3S245 2.7 15.5 1.0
CB B:CYS204 3.7 19.7 1.0
S4 B:F3S245 3.9 8.0 1.0
N B:PHE206 3.9 14.9 1.0
CA B:PHE206 4.1 13.3 1.0
CA B:CYS204 4.1 20.6 1.0
SG B:CYS158 4.2 9.2 1.0
N B:VAL207 4.2 11.3 1.0
CD1 B:ILE224 4.3 9.6 1.0
N B:THR205 4.3 17.8 1.0
C B:CYS204 4.5 19.3 1.0
C B:PHE206 4.6 13.3 1.0
N B:GLY208 4.9 13.6 1.0
C B:THR205 5.0 16.2 1.0

Iron binding site 4 out of 18 in 2b76

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Iron binding site 4 out of 18 in the E. Coli Quinol Fumarate Reductase Frda E49Q Mutation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 4 of E. Coli Quinol Fumarate Reductase Frda E49Q Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe245

b:13.1
occ:1.00
 FE3 B:F3S245 0.0 13.1 1.0
SG B:CYS158 2.0 9.2 1.0
S3 B:F3S245 2.2 11.6 1.0
S4 B:F3S245 2.3 8.0 1.0
S1 B:F3S245 2.3 15.1 1.0
FE4 B:F3S245 2.6 15.5 1.0
FE1 B:F3S245 2.6 24.5 1.0
CB B:CYS158 2.9 20.0 1.0
CA B:CYS158 3.6 21.6 1.0
S2 B:F3S245 3.7 11.5 1.0
C B:CYS158 4.4 22.4 1.0
CB B:VAL207 4.5 11.4 1.0
CB B:GLN160 4.6 13.8 1.0
SG B:CYS204 4.7 24.1 1.0
CG2 B:VAL207 4.7 12.8 1.0
CD B:PRO159 4.7 23.3 1.0
N B:VAL207 4.7 11.3 1.0
N B:CYS158 4.8 22.6 1.0
CG B:GLN160 4.8 18.8 1.0
N B:PRO159 4.9 21.0 1.0
SG B:CYS210 4.9 22.2 1.0

Iron binding site 5 out of 18 in 2b76

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Iron binding site 5 out of 18 in the E. Coli Quinol Fumarate Reductase Frda E49Q Mutation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 5 of E. Coli Quinol Fumarate Reductase Frda E49Q Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe245

b:15.5
occ:1.00
 FE4 B:F3S245 0.0 15.5 1.0
S4 B:F3S245 2.2 8.0 1.0
S3 B:F3S245 2.2 11.6 1.0
S2 B:F3S245 2.3 11.5 1.0
FE3 B:F3S245 2.6 13.1 1.0
SG B:CYS210 2.6 22.2 1.0
FE1 B:F3S245 2.7 24.5 1.0
CB B:CYS210 3.4 13.9 1.0
S1 B:F3S245 3.9 15.1 1.0
N B:CYS210 4.1 11.3 1.0
N B:GLY208 4.2 13.6 1.0
SG B:CYS158 4.3 9.2 1.0
CB B:ALA221 4.4 9.5 1.0
CA B:CYS210 4.4 13.4 1.0
CA B:GLY208 4.5 15.5 1.0
CB B:CYS158 4.6 20.0 1.0
SG B:CYS204 4.6 24.1 1.0
C B:GLY208 4.7 15.4 1.0
N B:TYR209 4.8 13.8 1.0
CD1 B:ILE224 4.8 9.6 1.0
CB B:PRO170 4.9 9.2 1.0
CA B:ALA221 4.9 9.2 1.0
N B:VAL207 5.0 11.3 1.0

Iron binding site 6 out of 18 in 2b76

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Iron binding site 6 out of 18 in the E. Coli Quinol Fumarate Reductase Frda E49Q Mutation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 6 of E. Coli Quinol Fumarate Reductase Frda E49Q Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe246

b:27.6
occ:1.00
 FE1 B:SF4246 0.0 27.6 1.0
S4 B:SF4246 2.2 21.2 1.0
SG B:CYS151 2.2 10.9 1.0
S2 B:SF4246 2.2 9.9 1.0
S3 B:SF4246 2.2 24.1 1.0
FE2 B:SF4246 2.6 19.5 1.0
FE4 B:SF4246 2.6 27.9 1.0
FE3 B:SF4246 2.6 23.9 1.0
CB B:CYS151 3.5 9.2 1.0
S1 B:SF4246 3.8 16.1 1.0
N B:CYS151 3.8 9.2 1.0
N B:GLY152 3.9 11.5 1.0
CD B:PRO215 4.0 18.1 1.0
CA B:CYS151 4.1 9.2 1.0
N B:LEU153 4.1 19.6 1.0
C B:CYS151 4.4 9.2 1.0
SG B:CYS154 4.5 12.6 1.0
SG B:CYS214 4.6 9.2 1.0
CG B:PRO215 4.6 18.0 1.0
SG B:CYS148 4.6 16.5 1.0
N B:CYS154 4.6 17.7 1.0
CB B:LEU153 4.6 19.4 1.0
CG1 B:ILE149 4.8 9.2 1.0
CA B:GLY152 4.8 14.8 1.0
CA B:LEU153 4.9 19.4 1.0
CG B:LEU153 4.9 18.2 1.0
N B:ASN150 4.9 9.2 1.0
C B:GLY152 4.9 17.7 1.0
C B:ASN150 4.9 9.2 1.0

Iron binding site 7 out of 18 in 2b76

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Iron binding site 7 out of 18 in the E. Coli Quinol Fumarate Reductase Frda E49Q Mutation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 7 of E. Coli Quinol Fumarate Reductase Frda E49Q Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe246

b:19.5
occ:1.00
 FE2 B:SF4246 0.0 19.5 1.0
S3 B:SF4246 2.2 24.1 1.0
SG B:CYS154 2.2 12.6 1.0
S1 B:SF4246 2.2 16.1 1.0
S4 B:SF4246 2.2 21.2 1.0
FE3 B:SF4246 2.5 23.9 1.0
FE4 B:SF4246 2.5 27.9 1.0
FE1 B:SF4246 2.6 27.6 1.0
CB B:CYS154 3.3 15.4 1.0
S2 B:SF4246 3.7 9.9 1.0
N B:CYS154 3.7 17.7 1.0
CA B:CYS154 4.1 16.5 1.0
CB B:ALA171 4.3 10.9 1.0
SG B:CYS148 4.4 16.5 1.0
SG B:CYS151 4.5 10.9 1.0
SG B:CYS214 4.6 9.2 1.0
N B:LEU153 4.7 19.6 1.0
CA B:ALA171 4.9 9.2 1.0
C B:LEU153 4.9 19.3 1.0
N B:GLY152 4.9 11.5 1.0
N B:ALA171 5.0 10.7 1.0

Iron binding site 8 out of 18 in 2b76

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Iron binding site 8 out of 18 in the E. Coli Quinol Fumarate Reductase Frda E49Q Mutation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 8 of E. Coli Quinol Fumarate Reductase Frda E49Q Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe246

b:23.9
occ:1.00
 FE3 B:SF4246 0.0 23.9 1.0
SG B:CYS148 2.2 16.5 1.0
S2 B:SF4246 2.2 9.9 1.0
S4 B:SF4246 2.2 21.2 1.0
S1 B:SF4246 2.2 16.1 1.0
FE2 B:SF4246 2.5 19.5 1.0
FE4 B:SF4246 2.6 27.9 1.0
FE1 B:SF4246 2.6 27.6 1.0
CB B:CYS148 3.3 12.9 1.0
S3 B:SF4246 3.7 24.1 1.0
CA B:CYS148 3.8 12.6 1.0
N B:ILE149 4.0 9.6 1.0
N B:ASN150 4.2 9.2 1.0
C B:CYS148 4.3 11.8 1.0
SG B:CYS154 4.4 12.6 1.0
CB B:ALA171 4.5 10.9 1.0
SG B:CYS214 4.6 9.2 1.0
N B:CYS151 4.7 9.2 1.0
SG B:CYS151 4.7 10.9 1.0
CA B:ASN150 4.8 9.2 1.0
C B:ILE149 5.0 9.2 1.0

Iron binding site 9 out of 18 in 2b76

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Iron binding site 9 out of 18 in the E. Coli Quinol Fumarate Reductase Frda E49Q Mutation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 9 of E. Coli Quinol Fumarate Reductase Frda E49Q Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Fe246

b:27.9
occ:1.00
 FE4 B:SF4246 0.0 27.9 1.0
S1 B:SF4246 2.2 16.1 1.0
S3 B:SF4246 2.2 24.1 1.0
SG B:CYS214 2.2 9.2 1.0
S2 B:SF4246 2.3 9.9 1.0
FE2 B:SF4246 2.5 19.5 1.0
FE3 B:SF4246 2.6 23.9 1.0
FE1 B:SF4246 2.6 27.6 1.0
CB B:CYS214 3.4 10.6 1.0
S4 B:SF4246 3.7 21.2 1.0
CA B:CYS214 3.8 10.9 1.0
CD B:PRO215 4.1 18.1 1.0
CG2 B:VAL218 4.5 14.8 1.0
SG B:CYS154 4.6 12.6 1.0
C B:CYS214 4.6 14.4 1.0
SG B:CYS151 4.6 10.9 1.0
N B:PRO215 4.6 17.5 1.0
SG B:CYS148 4.6 16.5 1.0
CB B:VAL218 4.7 15.9 1.0
N B:CYS214 5.0 9.8 1.0

Iron binding site 10 out of 18 in 2b76

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Iron binding site 10 out of 18 in the E. Coli Quinol Fumarate Reductase Frda E49Q Mutation


Mono view


Stereo pair view

A full contact list of Iron with other atoms in the Fe binding site number 10 of E. Coli Quinol Fumarate Reductase Frda E49Q Mutation within 5.0Å range:
probe atom residue distance (Å) B Occ
N:Fe244

b:44.8
occ:1.00
 FE1 N:FES244 0.0 44.8 1.0
SG N:CYS77 2.2 37.3 1.0
SG N:CYS65 2.3 55.6 1.0
S2 N:FES244 2.3 21.8 1.0
S1 N:FES244 2.3 24.2 1.0
FE2 N:FES244 2.8 53.1 1.0
CB N:CYS77 3.2 50.5 1.0
CB N:CYS65 3.4 40.9 1.0
N N:CYS77 4.0 49.6 1.0
N N:CYS65 4.0 24.4 1.0
CA N:ALA60 4.2 41.1 1.0
CA N:CYS77 4.2 42.7 1.0
N N:ALA60 4.2 54.5 1.0
SG N:CYS57 4.2 65.8 1.0
CA N:CYS65 4.3 42.7 1.0
CB N:LEU75 4.4 0.7 1.0
O N:LEU75 4.4 23.8 1.0
N N:SER64 4.6 12.3 1.0
C N:LEU75 4.6 23.1 1.0
CD1 N:LEU37 4.7 87.5 1.0
SG N:CYS62 4.7 58.7 1.0
N N:ILE61 4.7 55.8 1.0
CB N:SER64 4.9 36.2 1.0
C N:SER64 4.9 15.7 1.0
CA N:LEU75 4.9 0.7 1.0
C N:CYS77 4.9 52.1 1.0
CD1 N:LEU75 4.9 0.7 1.0
CA N:SER64 5.0 23.7 1.0

Reference:

E.Maklashina, T.M.Iverson, Y.Sher, V.Kotlyar, J.Andrell, O.Mirza, J.M.Hudson, F.A.Armstrong, R.A.Rothery, J.H.Weiner, G.Cecchini. Fumarate Reductase and Succinate Oxidase Activity of Escherichia Coli Complex II Homologs Are Perturbed Differently By Mutation of the Flavin Binding Domain J.Biol.Chem. V. 281 11357 2006.
ISSN: ISSN 0021-9258
PubMed: 16484232
DOI: 10.1074/JBC.M512544200
Page generated: Sat Aug 3 19:31:52 2024

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