|Entry||Database: PDB / ID: 1tl4|
|Title||Solution structure of Cu(I) HAH1|
|Components||Copper transport protein ATOX1|
|Keywords||METAL TRANSPORT / copper protein / copper chaperone / Menkes / Wilson / Structural Proteomics in Europe / SPINE / Structural Genomics|
|Function / homology|
Function and homology information
metallochaperone activity / Ion influx/efflux at host-pathogen interface / copper-dependent protein binding / copper chaperone activity / copper ion export / copper ion transport / cuprous ion binding / Detoxification of Reactive Oxygen Species / cellular copper ion homeostasis / response to oxidative stress ...metallochaperone activity / Ion influx/efflux at host-pathogen interface / copper-dependent protein binding / copper chaperone activity / copper ion export / copper ion transport / cuprous ion binding / Detoxification of Reactive Oxygen Species / cellular copper ion homeostasis / response to oxidative stress / ATPase binding / copper ion binding / negative regulation of apoptotic process / cytosol
Similarity search - Function
Heavy-metal-associated domain. / Heavy-metal-associated, conserved site / Heavy-metal-associated domain / Heavy-metal-associated domain profile. / Heavy metal-associated domain superfamily / Heavy metal-associated domain, HMA / Alpha-Beta Plaits - #100 / Alpha-Beta Plaits / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
COPPER (I) ION / Copper transport protein ATOX1
Similarity search - Component
|Biological species||Homo sapiens (human)|
|Method||SOLUTION NMR / torsion angle dynamics, simulated annealing, restrained energy minimization|
|Authors||Anastassopoulou, I. / Banci, L. / Bertini, I. / Cantini, F. / Katsari, E. / Rosato, A. / Structural Proteomics in Europe (SPINE)|
|Citation||Journal: Biochemistry / Year: 2004|
Title: Solution Structure of the Apo and Copper(I)-Loaded Human Metallochaperone HAH1.
Authors: Anastassopoulou, I. / Banci, L. / Bertini, I. / Cantini, F. / Katsari, E. / Rosato, A.
|Structure viewer||Molecule: |
Downloads & links
A: Copper transport protein ATOX1
|#1: Protein|| |
Mass: 7412.646 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ATOX1, HAH1 / Plasmid: pET20b+ / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS / References: UniProt: O00244
|#2: Chemical|| ChemComp-CU1 / |
|Experiment||Method: SOLUTION NMR|
|Radiation||Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M|
|Radiation wavelength||Relative weight: 1|
|Refinement||Method: torsion angle dynamics, simulated annealing, restrained energy minimization|
Software ordinal: 1
Details: the structures were based on a total of 1219 meaningful distance constraints, 99 dihedral angle restraints.
|NMR ensemble||Conformer selection criteria: target function / Conformers calculated total number: 400 / Conformers submitted total number: 30|
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