Atomistry » Copper » PDB 1oe2-1rjp » 1uux
Atomistry »
  Copper »
    PDB 1oe2-1rjp »
      1uux »

Copper in PDB 1uux: Structure of A Molybdopterin-Bound CNX1G Domain Links Molybdenum and Copper Metabolism

Protein crystallography data

The structure of Structure of A Molybdopterin-Bound CNX1G Domain Links Molybdenum and Copper Metabolism, PDB code: 1uux was solved by J.Kuper, A.Llamas, H.J.Hecht, R.R.Mendel, G.Schwarz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 20.00 / 1.6
Space group F 41 3 2
Cell size a, b, c (Å), α, β, γ (°) 171.034, 171.034, 171.034, 90.00, 90.00, 90.00
R / Rfree (%) 16.4 / 19.1

Copper Binding Sites:

The binding sites of Copper atom in the Structure of A Molybdopterin-Bound CNX1G Domain Links Molybdenum and Copper Metabolism (pdb code 1uux). This binding sites where shown within 5.0 Angstroms radius around Copper atom.
In total only one binding site of Copper was determined in the Structure of A Molybdopterin-Bound CNX1G Domain Links Molybdenum and Copper Metabolism, PDB code: 1uux:

Copper binding site 1 out of 1 in 1uux

Go back to Copper Binding Sites List in 1uux
Copper binding site 1 out of 1 in the Structure of A Molybdopterin-Bound CNX1G Domain Links Molybdenum and Copper Metabolism


Mono view


Stereo pair view

A full contact list of Copper with other atoms in the Cu binding site number 1 of Structure of A Molybdopterin-Bound CNX1G Domain Links Molybdenum and Copper Metabolism within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Cu1168

b:17.3
occ:0.70
S1' A:MTE1164 2.3 13.2 0.7
S2' A:MTE1164 2.3 10.7 0.7
C1' A:MTE1164 3.0 13.4 0.7
C2' A:MTE1164 3.2 14.9 0.7
CD2 A:PHE118 4.3 25.5 0.5
C6 A:MTE1164 4.3 14.6 0.7
CD1 A:LEU121 4.7 15.0 1.0
C3' A:MTE1164 4.7 11.8 0.7
CB A:PHE118 4.8 17.9 1.0
CG A:PHE118 5.0 20.8 0.5

Reference:

J.Kuper, A.Llamas, H.J.Hecht, R.R.Mendel, G.Schwarz. Structure of A Molybdopterin-Bound CNX1G Domain Links Molybdenum and Copper Metabolism Nature V. 430 803 2004.
ISSN: ISSN 0028-0836
PubMed: 15306815
DOI: 10.1038/NATURE02681
Page generated: Thu Sep 3 16:21:37 2020
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy