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Molybdenum 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:

Iron (Fe) 8 atoms

Molybdenum Binding Sites:

The binding sites of Molybdenum 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 Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Crystal Structure of Quinoline 2-Oxidoreductase From Pseudomonas Putida 86, PDB code: 1t3q:
Jump to Molybdenum binding site number: 1; 2;

Molybdenum binding site 1 out of 2 in 1t3q

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


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo 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
B:Mo4923

b:26.8
occ:1.00
MO B:SMO4923 0.0 26.8 1.0
OM1 B:SMO4923 1.7 27.7 1.0
OM2 B:SMO4923 1.7 28.8 1.0
S B:SMO4923 2.1 28.7 1.0
S8' B:MCN4921 2.4 26.7 1.0
S7' B:MCN4921 2.4 23.5 1.0
C7' B:MCN4921 3.4 24.7 1.0
C8' B:MCN4921 3.4 24.7 1.0
N B:ALA546 3.8 24.5 1.0
OE2 B:GLU743 4.0 27.1 1.0
CA B:GLY256 4.0 17.0 1.0
CA B:TYR545 4.1 26.9 1.0
N B:GLY256 4.1 16.1 1.0
CD B:GLU743 4.2 27.2 1.0
C B:PHE255 4.4 14.6 1.0
CB B:TYR545 4.4 26.2 1.0
CG B:GLU743 4.4 23.5 1.0
C B:TYR545 4.5 25.2 1.0
O B:PHE255 4.5 14.3 1.0
CA B:ARG371 4.5 14.7 1.0
N B:ARG371 4.6 14.1 1.0
NE2 B:GLN224 4.7 20.2 1.0
O1 B:GOL3902 4.7 51.2 1.0
CA B:ALA546 4.8 25.1 1.0
C1 B:GOL3902 4.8 52.4 1.0
OE1 B:GLU743 4.9 28.3 1.0
C6' B:MCN4921 4.9 20.0 1.0
C9' B:MCN4921 4.9 23.7 1.0

Molybdenum binding site 2 out of 2 in 1t3q

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


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo 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
E:Mo4922

b:27.9
occ:1.00
MO E:SMO4922 0.0 27.9 1.0
OM1 E:SMO4922 1.7 28.8 1.0
OM2 E:SMO4922 1.8 29.8 1.0
S E:SMO4922 2.1 28.8 1.0
S8' E:MCN4920 2.4 25.3 1.0
S7' E:MCN4920 2.4 22.7 1.0
C7' E:MCN4920 3.4 25.3 1.0
C8' E:MCN4920 3.4 25.5 1.0
N E:ALA546 3.8 28.1 1.0
O E:HOH5252 3.9 42.6 1.0
CA E:GLY256 4.0 16.0 1.0
CA E:TYR545 4.1 29.7 1.0
OE2 E:GLU743 4.1 27.3 1.0
N E:GLY256 4.1 16.2 1.0
CD E:GLU743 4.3 27.1 1.0
C E:PHE255 4.4 15.2 1.0
CB E:TYR545 4.4 29.8 1.0
C E:TYR545 4.4 28.5 1.0
CG E:GLU743 4.4 26.5 1.0
O E:PHE255 4.5 16.3 1.0
CA E:ARG371 4.6 17.6 1.0
NE2 E:GLN224 4.6 20.6 1.0
N E:ARG371 4.6 17.3 1.0
CA E:ALA546 4.8 25.1 1.0
C6' E:MCN4920 4.8 25.4 1.0
C9' E:MCN4920 4.9 25.3 1.0
OE1 E:GLU743 4.9 29.6 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: Tue Dec 15 05:16:36 2020

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