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Iron in PDB 1t3q: Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86

Enzymatic activity of Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86

All present enzymatic activity of Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86:
1.3.99.17;

Protein crystallography data

The structure of Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86, PDB code: 1t3q was solved by I.Bonin, B.M.Martins, V.Purvanov, S.Fetzner, R.Huber, H.Dobbek, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 19.29 / 1.80
Space group C 1 2 1
Cell size a, b, c (Å), α, β, γ (°) 278.320, 72.100, 202.650, 90.00, 127.98, 90.00
R / Rfree (%) 18.6 / 20.7

Other elements in 1t3q:

The structure of Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86 also contains other interesting chemical elements:

Molybdenum (Mo) 2 atoms

Iron Binding Sites:

The binding sites of Iron atom in the Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86 (pdb code 1t3q). This binding sites where shown within 5.0 Angstroms radius around Iron atom.
In total 8 binding sites of Iron where determined in the Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86, PDB code: 1t3q:
Jump to Iron binding site number: 1; 2; 3; 4; 5; 6; 7; 8;

Iron binding site 1 out of 8 in 1t3q

Go back to Iron Binding Sites List in 1t3q
Iron binding site 1 out of 8 in the Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86


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 Quinoline 2-Oxidoreductase From Pseudomonas Putida 86 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe4907

b:14.9
occ:1.00
FE1 A:FES4907 0.0 14.9 1.0
S2 A:FES4907 2.2 18.6 1.0
S1 A:FES4907 2.3 15.3 1.0
SG A:CYS107 2.3 16.9 1.0
SG A:CYS144 2.4 15.5 1.0
FE2 A:FES4907 2.7 16.3 1.0
CB A:CYS144 3.2 17.1 1.0
CB A:CYS107 3.4 15.7 1.0
N A:CYS107 3.6 12.8 1.0
N A:GLY108 3.8 12.7 1.0
O B:HOH4927 3.9 17.2 1.0
CA A:CYS107 3.9 14.2 1.0
N A:CYS144 4.1 16.2 1.0
C A:CYS107 4.3 13.6 1.0
N A:PHE109 4.3 14.5 1.0
CA A:CYS144 4.3 17.2 1.0
SG A:CYS142 4.4 17.9 1.0
C A:GLN106 4.7 12.6 1.0
SG A:CYS110 4.7 15.1 1.0
CA A:GLY108 4.7 14.3 1.0
CB A:GLN106 4.8 14.4 1.0
N A:ARG143 4.8 15.3 1.0
N A:GLN106 4.9 14.3 1.0
N A:CYS110 4.9 14.5 1.0
CB A:PHE109 4.9 16.4 1.0
C A:GLY108 5.0 14.4 1.0

Iron binding site 2 out of 8 in 1t3q

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Iron binding site 2 out of 8 in the Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86


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 Quinoline 2-Oxidoreductase From Pseudomonas Putida 86 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe4907

b:16.3
occ:1.00
FE2 A:FES4907 0.0 16.3 1.0
S1 A:FES4907 2.2 15.3 1.0
S2 A:FES4907 2.2 18.6 1.0
SG A:CYS110 2.3 15.1 1.0
SG A:CYS142 2.4 17.9 1.0
FE1 A:FES4907 2.7 14.9 1.0
CB A:CYS142 3.4 15.4 1.0
CB A:CYS110 3.4 14.3 1.0
CA A:CYS142 3.7 15.3 1.0
N A:CYS110 4.1 14.5 1.0
N A:ARG143 4.2 15.3 1.0
CB A:CYS144 4.3 17.1 1.0
C A:CYS142 4.4 13.7 1.0
CA A:CYS110 4.4 14.8 1.0
N A:CYS144 4.4 16.2 1.0
O A:HOH4914 4.6 14.8 1.0
SG A:CYS144 4.6 15.5 1.0
CG2 A:THR145 4.6 14.9 1.0
SG A:CYS107 4.7 16.9 1.0
O A:LEU141 4.9 16.2 1.0
CA A:CYS144 4.9 17.2 1.0
N A:CYS142 5.0 16.8 1.0
N A:PHE109 5.0 14.5 1.0

Iron binding site 3 out of 8 in 1t3q

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Iron binding site 3 out of 8 in the Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86


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 Quinoline 2-Oxidoreductase From Pseudomonas Putida 86 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe4908

b:16.1
occ:1.00
FE1 A:FES4908 0.0 16.1 1.0
S2 A:FES4908 2.2 17.3 1.0
S1 A:FES4908 2.3 18.3 1.0
SG A:CYS53 2.3 16.8 1.0
SG A:CYS48 2.4 18.0 1.0
FE2 A:FES4908 2.7 17.1 1.0
N A:CYS48 3.5 17.6 1.0
CB A:CYS53 3.6 17.1 1.0
N A:CYS53 3.6 15.9 1.0
CB A:CYS48 3.6 16.8 1.0
N A:GLY54 3.7 14.6 1.0
N A:GLU49 3.7 18.4 1.0
CA A:CYS53 3.9 16.9 1.0
CA A:CYS48 3.9 17.8 1.0
OG A:SER55 4.2 23.5 1.0
C A:CYS53 4.2 16.1 1.0
N A:GLY47 4.2 15.9 1.0
C A:GLY47 4.3 19.4 1.0
C A:CYS48 4.3 19.0 1.0
N A:SER55 4.3 14.6 1.0
N A:VAL52 4.4 16.6 1.0
N A:GLY51 4.4 19.0 1.0
SG A:CYS68 4.5 17.4 1.0
CA A:GLY47 4.6 18.7 1.0
C A:VAL52 4.6 17.8 1.0
N A:GLN50 4.6 19.4 1.0
CA A:GLU49 4.7 20.1 1.0
SG A:CYS56 4.7 15.0 1.0
CA A:GLY54 4.7 13.9 1.0
C A:GLY51 4.7 19.4 1.0
CA A:GLY51 4.8 19.3 1.0
C A:GLY54 5.0 14.4 1.0
N A:CYS56 5.0 14.8 1.0

Iron binding site 4 out of 8 in 1t3q

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Iron binding site 4 out of 8 in the Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86


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 Quinoline 2-Oxidoreductase From Pseudomonas Putida 86 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Fe4908

b:17.1
occ:1.00
FE2 A:FES4908 0.0 17.1 1.0
S1 A:FES4908 2.1 18.3 1.0
S2 A:FES4908 2.3 17.3 1.0
SG A:CYS56 2.3 15.0 1.0
SG A:CYS68 2.4 17.4 1.0
FE1 A:FES4908 2.7 16.1 1.0
CB A:CYS68 3.2 16.9 1.0
CB A:CYS56 3.4 13.9 1.0
N A:CYS56 4.2 14.8 1.0
N A:CYS68 4.3 17.3 1.0
N A:GLY51 4.3 19.0 1.0
CA A:CYS68 4.4 18.3 1.0
N A:GLU49 4.4 18.4 1.0
CA A:GLY51 4.4 19.3 1.0
CA A:CYS56 4.4 13.9 1.0
SG A:CYS48 4.4 18.0 1.0
CB A:ARG66 4.6 15.7 1.0
CA A:GLU49 4.6 20.1 1.0
CD A:ARG66 4.6 17.8 1.0
SG A:CYS53 4.7 16.8 1.0
N A:GLY54 4.8 14.6 1.0
N A:GLN50 4.9 19.4 1.0

Iron binding site 5 out of 8 in 1t3q

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Iron binding site 5 out of 8 in the Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86


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 Quinoline 2-Oxidoreductase From Pseudomonas Putida 86 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe4909

b:16.7
occ:1.00
FE1 D:FES4909 0.0 16.7 1.0
S1 D:FES4909 2.2 17.2 1.0
S2 D:FES4909 2.2 16.7 1.0
SG D:CYS107 2.4 16.6 1.0
SG D:CYS144 2.5 18.8 1.0
FE2 D:FES4909 2.6 17.0 1.0
CB D:CYS144 3.3 19.6 1.0
CB D:CYS107 3.4 13.6 1.0
N D:CYS107 3.6 15.7 1.0
N D:GLY108 3.8 16.4 1.0
CA D:CYS107 3.9 16.2 1.0
O E:HOH4932 4.0 15.7 1.0
N D:CYS144 4.0 18.9 1.0
C D:CYS107 4.3 16.5 1.0
N D:PHE109 4.3 15.5 1.0
SG D:CYS142 4.3 17.4 1.0
CA D:CYS144 4.3 18.5 1.0
N D:ARG143 4.7 17.6 1.0
SG D:CYS110 4.7 18.4 1.0
C D:GLN106 4.8 14.9 1.0
CA D:GLY108 4.8 15.4 1.0
N D:CYS110 4.9 18.0 1.0
N D:GLN106 4.9 14.8 1.0
CB D:PHE109 4.9 15.9 1.0
C D:ARG143 4.9 18.1 1.0
CB D:GLN106 4.9 16.7 1.0
C D:GLY108 5.0 16.3 1.0

Iron binding site 6 out of 8 in 1t3q

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Iron binding site 6 out of 8 in the Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86


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 Quinoline 2-Oxidoreductase From Pseudomonas Putida 86 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe4909

b:17.0
occ:1.00
FE2 D:FES4909 0.0 17.0 1.0
S1 D:FES4909 2.2 17.2 1.0
S2 D:FES4909 2.2 16.7 1.0
SG D:CYS110 2.3 18.4 1.0
SG D:CYS142 2.4 17.4 1.0
FE1 D:FES4909 2.6 16.7 1.0
CB D:CYS142 3.4 14.2 1.0
CB D:CYS110 3.4 17.2 1.0
CA D:CYS142 3.7 14.8 1.0
N D:CYS110 4.0 18.0 1.0
N D:ARG143 4.1 17.6 1.0
CA D:CYS110 4.3 16.2 1.0
C D:CYS142 4.4 15.9 1.0
N D:CYS144 4.4 18.9 1.0
O D:HOH4918 4.5 15.5 1.0
CB D:CYS144 4.5 19.6 1.0
SG D:CYS144 4.6 18.8 1.0
SG D:CYS107 4.6 16.6 1.0
CG2 D:THR145 4.9 16.7 1.0
N D:PHE109 4.9 15.5 1.0
O D:LEU141 4.9 18.2 1.0
C D:CYS110 5.0 17.4 1.0
N D:GLY108 5.0 16.4 1.0

Iron binding site 7 out of 8 in 1t3q

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Iron binding site 7 out of 8 in the Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86


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 Quinoline 2-Oxidoreductase From Pseudomonas Putida 86 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe4910

b:16.8
occ:1.00
FE1 D:FES4910 0.0 16.8 1.0
S2 D:FES4910 2.2 14.7 1.0
S1 D:FES4910 2.2 15.3 1.0
SG D:CYS53 2.3 17.3 1.0
SG D:CYS48 2.4 18.2 1.0
FE2 D:FES4910 2.8 17.1 1.0
N D:CYS48 3.5 18.8 1.0
CB D:CYS53 3.5 14.6 1.0
N D:CYS53 3.5 18.1 1.0
CB D:CYS48 3.6 16.7 1.0
N D:GLY54 3.7 16.7 1.0
N D:GLU49 3.8 20.5 1.0
CA D:CYS53 3.9 16.4 1.0
CA D:CYS48 3.9 18.6 1.0
OG D:SER55 4.1 23.8 1.0
C D:CYS53 4.2 18.1 1.0
N D:GLY47 4.2 18.9 1.0
C D:GLY47 4.2 19.8 1.0
N D:SER55 4.3 17.1 1.0
C D:CYS48 4.3 19.4 1.0
N D:VAL52 4.3 18.1 1.0
N D:GLY51 4.4 21.1 1.0
CA D:GLY47 4.5 18.5 1.0
SG D:CYS68 4.5 17.5 1.0
C D:VAL52 4.6 18.7 1.0
N D:GLN50 4.7 19.5 1.0
CA D:GLY54 4.7 16.2 1.0
SG D:CYS56 4.7 17.3 1.0
C D:GLY51 4.7 19.6 1.0
CA D:GLY51 4.7 19.4 1.0
CA D:GLU49 4.8 20.8 1.0
C D:GLY54 4.9 15.9 1.0
CB D:SER55 4.9 19.7 1.0
N D:CYS56 5.0 15.2 1.0
CA D:VAL52 5.0 18.8 1.0

Iron binding site 8 out of 8 in 1t3q

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Iron binding site 8 out of 8 in the Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86


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 Quinoline 2-Oxidoreductase From Pseudomonas Putida 86 within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Fe4910

b:17.1
occ:1.00
FE2 D:FES4910 0.0 17.1 1.0
S1 D:FES4910 2.2 15.3 1.0
S2 D:FES4910 2.3 14.7 1.0
SG D:CYS56 2.4 17.3 1.0
SG D:CYS68 2.4 17.5 1.0
FE1 D:FES4910 2.8 16.8 1.0
CB D:CYS68 3.2 16.3 1.0
CB D:CYS56 3.4 15.7 1.0
N D:CYS68 4.2 17.6 1.0
N D:GLY51 4.2 21.1 1.0
N D:CYS56 4.3 15.2 1.0
CA D:CYS68 4.3 17.8 1.0
CA D:GLY51 4.3 19.4 1.0
N D:GLU49 4.4 20.5 1.0
SG D:CYS48 4.4 18.2 1.0
CA D:CYS56 4.4 15.3 1.0
CA D:GLU49 4.6 20.8 1.0
CB D:ARG66 4.6 18.4 1.0
CD D:ARG66 4.7 19.4 1.0
SG D:CYS53 4.8 17.3 1.0
N D:GLN50 4.9 19.5 1.0
N D:GLY54 4.9 16.7 1.0
OG D:SER55 5.0 23.8 1.0

Reference:

I.Bonin, B.M.Martins, V.Purvanov, S.Fetzner, R.Huber, H.Dobbek. Active Site Geometry and Substrate Recognition of the Molybdenum Hydroxylase Quinoline 2-Oxidoreductase. Structure V. 12 1425 2004.
ISSN: ISSN 0969-2126
PubMed: 15296736
DOI: 10.1016/J.STR.2004.05.014
Page generated: Sat Aug 3 15:08:17 2024

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