Atomistry » Molybdenum » PDB 4c80-5koj » 4uhx
Atomistry »
  Molybdenum »
    PDB 4c80-5koj »
      4uhx »

Molybdenum in PDB 4uhx: Human Aldehyde Oxidase in Complex with Phthalazine and Thioridazine

Enzymatic activity of Human Aldehyde Oxidase in Complex with Phthalazine and Thioridazine

All present enzymatic activity of Human Aldehyde Oxidase in Complex with Phthalazine and Thioridazine:
1.2.3.1;

Protein crystallography data

The structure of Human Aldehyde Oxidase in Complex with Phthalazine and Thioridazine, PDB code: 4uhx was solved by C.Coelho, M.J.Romao, T.Santos-Silva, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 105.17 / 2.70
Space group P 42 21 2
Cell size a, b, c (Å), α, β, γ (°) 148.732, 148.732, 132.808, 90.00, 90.00, 90.00
R / Rfree (%) 19.526 / 24.408

Other elements in 4uhx:

The structure of Human Aldehyde Oxidase in Complex with Phthalazine and Thioridazine also contains other interesting chemical elements:

Iron (Fe) 4 atoms

Molybdenum Binding Sites:

The binding sites of Molybdenum atom in the Human Aldehyde Oxidase in Complex with Phthalazine and Thioridazine (pdb code 4uhx). This binding sites where shown within 5.0 Angstroms radius around Molybdenum atom.
In total only one binding site of Molybdenum was determined in the Human Aldehyde Oxidase in Complex with Phthalazine and Thioridazine, PDB code: 4uhx:

Molybdenum binding site 1 out of 1 in 4uhx

Go back to Molybdenum Binding Sites List in 4uhx
Molybdenum binding site 1 out of 1 in the Human Aldehyde Oxidase in Complex with Phthalazine and Thioridazine


Mono view


Stereo pair view

A full contact list of Molybdenum with other atoms in the Mo binding site number 1 of Human Aldehyde Oxidase in Complex with Phthalazine and Thioridazine within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mo3004

b:0.4
occ:1.00
 MO A:MOS3004 0.0 0.4 1.0
O2 A:MOS3004 1.7 0.5 1.0
O1 A:MOS3004 2.0 0.9 1.0
S1' A:MTE3003 2.3 86.9 1.0
S A:MOS3004 2.3 1.0 0.7
S2' A:MTE3003 2.5 88.4 1.0
C1' A:MTE3003 3.3 85.7 1.0
C2' A:MTE3003 3.4 87.2 1.0
OE2 A:GLU1270 3.7 73.7 1.0
N A:GLY1088 3.9 73.0 1.0
CA A:GLY1087 4.0 68.2 1.0
CD A:GLU1270 4.3 74.3 1.0
NE2 A:GLN776 4.5 60.2 1.0
N A:GLY808 4.5 59.2 1.0
C A:GLY1087 4.5 71.2 1.0
N A:ARG921 4.6 66.4 1.0
CG A:GLU1270 4.6 73.9 1.0
CA A:ARG921 4.7 67.0 1.0
CA A:GLY808 4.7 59.9 1.0
C A:PHE807 4.7 59.5 1.0
C6 A:MTE3003 4.7 85.1 1.0
C3' A:MTE3003 4.8 87.5 1.0
C A:PHE920 4.9 67.2 1.0
OE1 A:GLU1270 5.0 75.5 1.0
CA A:GLY1088 5.0 73.8 1.0
O A:PHE807 5.0 60.4 1.0

Reference:

C.Coelho, A.Foti, T.Hartmann, T.Santos-Silva, S.Leimkuhler, M.J.Romao. Structural Insights Into Xenobiotic and Inhibitor Binding to Human Aldehyde Oxidase Nat.Chem.Biol. V. 11 779 2015.
ISSN: ISSN 1552-4450
PubMed: 26322824
DOI: 10.1038/NCHEMBIO.1895
Page generated: Sun Oct 6 16:12:47 2024

Last articles

Zn in 9J0N
Zn in 9J0O
Zn in 9J0P
Zn in 9FJX
Zn in 9EKB
Zn in 9C0F
Zn in 9CAH
Zn in 9CH0
Zn in 9CH3
Zn in 9CH1
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy