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Structure paper

TitleMolecular recognition and maturation of SOD1 by its evolutionarily destabilised cognate chaperone hCCS.
Journal, issue, pagesPlos Biol., Vol. 17, Page e3000141-e3000141, Year 2019
Publish dateFeb 2, 2018 (structure data deposition date)
AuthorsSala, F.A. / Wright, G.S.A. / Antonyuk, S.V. / Garratt, R.C. / Hasnain, S.S.
External linksPlos Biol. / PubMed:30735496
MethodsX-ray diffraction
Resolution1.55 - 3.05 Å
Structure data

PDB-6fn8:
Domain II of the HUMAN COPPER CHAPERONE FOR SUPEROXIDE DISMUTASE at 1.55 A resolution
Method: X-RAY DIFFRACTION / Resolution: 1.55 Å

PDB-6foi:
Human Cys57/156Ala superoxide dismutase-1 (SOD1), as isolated.
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-6fol:
Domain II of the human copper chaperone in complex with human Cu,Zn superoxide dismutase
Method: X-RAY DIFFRACTION / Resolution: 2.55 Å

PDB-6fon:
Elongated conformer of the human copper chaperone for SOD1 complexed with human SOD1
Method: X-RAY DIFFRACTION / Resolution: 3.05 Å

PDB-6fp6:
Complex of human Cu,Zn SOD1 with the human copper chaperone for SOD1 in a compact conformation
Method: X-RAY DIFFRACTION / Resolution: 3 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

ChemComp-PE8:
3,6,9,12,15,18,21-HEPTAOXATRICOSANE-1,23-DIOL

ChemComp-GOL:
GLYCEROL

ChemComp-PPI:
PROPANOIC ACID

Source
  • homo sapiens (human)
KeywordsCHAPERONE / ImgG-like / copper-chaperone / zinc-binding / protein maturation / OXIDOREDUCTASE / zinc / copper / disulphide mutant / METAL BINDING PROTEIN / heterodimer / hSOD1

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