Atomistry » Iron » PDB 1su6-1tfd » 1t3q
Atomistry »
  Iron »
    PDB 1su6-1tfd »
      1t3q »

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

Go back to Iron Binding Sites List in 1t3q
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

Go back to Iron Binding Sites List in 1t3q
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

Go back to Iron Binding Sites List in 1t3q
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

Go back to Iron Binding Sites List in 1t3q
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

Go back to Iron Binding Sites List in 1t3q
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

Go back to Iron Binding Sites List in 1t3q
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

Go back to Iron Binding Sites List in 1t3q
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

Last articles

Zn in 9JYW
Zn in 9IR4
Zn in 9IR3
Zn in 9GMX
Zn in 9GMW
Zn in 9JEJ
Zn in 9ERF
Zn in 9ERE
Zn in 9EGV
Zn in 9EGW
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy