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Database of Copper-Chelating Proteins

 
   
 

The networks of copper metabolism

Copper transport at the cell surface and the delivery of copper into intracellular compartments depend on a series of membrane proteins and small soluble peptides, the copper chaperones. Many integral membrane proteins such as Fre(Ferric ion reductase enzyme) and CTR(Copper transporter protein) form the channels to assist the permeation of the ions through the plasm membranes. The chaperones, for example, ATX1(Anti-oxidant 1), COX17(Cytochrome oxidase 17 copper chaperone) and LYS7(Lysine biosynthesis 7) specially bind and hand copper ions to their target proteins. All these proteins comprise a functionally integrated system for maintaining cellular copper homeostasis.
Figure 1. Contents of hydrophilic (a, b) and hydrophobic (c, d) amino acids of proteins in DCCP_3D (a, c) and the same amount of general proteins selected from PDB (b, d)
Table 1. The statistical features of hydrophilic and hydrophobic amino acids contents of copper-chelating proteins and general proteins
Table 2. Secondary structure prediction accuracies of copper-chelating proteins in DCCP_3D based on five widely-used secondary-structure-predicting software
Table 3. SCOP classifications of copper-chelating proteins in DCCP_3D and general proteins selected from PDB
Table 4. Calculated binding-energies of the proteins involved in the transportation of copper ions from outside to inside of cell
Figure 1. Contents of hydrophilic (a, b) and hydrophobic (c, d) amino acids of proteins in DCCP_3D (a, c) and the same amount of general proteins selected from PDB (b, d)    [Top]

Table 1. The statistical features of hydrophilic and hydrophobic amino acids contents of copper-chelating proteins and general proteins    [Top]
Statistical parameters Hydrophilic amino acids content Hydrophobic amino acids content
Copper-chelating proteins General proteins Copper-chelating proteins General proteins
Average 0.4395 0.4769 0.4676 0.4595
Standard deviation 0.0627 0.0627 0.0592 0.0558
Skew -0.9117 -0.1816 0.2639 0.0219

Table 2. Secondary structure prediction accuracies of copper-chelating proteins in DCCP_3D based on five widely-used secondary-structure-predicting software    [Top]
 
Copper-chelating proteins
Criterion 1*
Criterion 2*
Criterion 3*
Average accuracy for General proteins
PHD
PROF
NNPREDICT
PSIPRED
JPRED
74.82 74.83 75.82
76.92 76.94 77.73
60.60 60.60 61.69
79.13 79.13 79.90
74.54 74.56 75.80
71.9-73.5
>78
>65
78-80.6
72.9-74.8
    * Conversion criteria from 8 types to 3 types
  1. H, G, I--H£» E, B--E£» other--C.
  2. H, G--H£» E, B--E£» other--C.
  3. H, G--H£» E--E£» other--C.

Table 3. SCOP classifications of copper-chelating proteins in DCCP_3D and general proteins selected from PDB    [Top]
SCOP classification£¨domain£© Copper-chelating proteins General proteins
All alpha proteins
182
159
All beta protein
913
505
Alpha and beta proteins (a/b)
103
346
Alpha and beta proteins (a+b)
225
250
Multi-domain proteins (alpha and beta)
8
24
Membrane and cell surface proteins and peptides
112
14
Small proteins
45
28
Coiled coil proteins
0
19
Low resolution protein structures
45
1
Peptides
1
0
Designed proteins
0
0

Table 4. Calculated binding-energies of the proteins involved in the transportation of copper ions from outside to inside of cell    [Top]
Protein Name
PDB ID
pH
Resolution
Binding Energy
Cellular Localization
Peptidylglycine
3PHM
5.5
2.10
401.16
Excreted
Peptidylglycine
1OPM
5.5
2.10
403.71
Excreted
Azurin
1A4A
6.5
1.89
608.40
Periplasm
Auracyanin
1QHQ
7.0
1.55
713.61
Peripheral membrane
Pseudoazurin
3PAZ
7.0
1.73
713.73
Periplasm
Dissimilatory nitrite reductase
1HAW
8.5
1.90
717.57
Periplasm
Pseudoazurin
4PAZ
7.0
1.76
723.44
Periplasm
Azurin ii
1DZO
6.0
1.75
723.62
Periplasm
Azurin
1JZF
7.0
1.50
725.10
Periplasm
Azurin ii
1DYZ
6.0
1.75
726.90
Periplasm
Plastocyanin
1BYO
5.5
2.00
738.37
Chloroplast
Plastocyanin
1BYP
7.0
1.75
748.84
Chloroplast
Superoxide dismutase
1SPD
-
2.40
1170.61
Cytoplasm
Cu, Zn superoxide dismutase
1XSO
-
1.49
1322.56
Cytoplasm


 
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Last updated on June 25, 2005!

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