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PDBe Entry: 2gfo 
Structure of the Catalytic Domain of Human Ubiquitin Carboxyl-terminal Hydrolase 8
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HYDROLASE
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X-RAY DIFFRACTION
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Resolution: 2.0 Å, R-factor: 17.056%, Free R-factor: 21.023%, Spacegroup: P 61
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04/04/2006, deposition: 22/03/2006, last revision: 24/02/2009
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Walker, J.R.; Avvakumov, G.V; Xue, S.; Newman, E.M.; Finerty Jr., P.J.; Butler-Cole, C.; Weigelt, J.; Sundstrom, M.; Arrowsmith, C.; Edwards, A.; Bochkarev, A.; Dhe-Paganon, S.; Structural Genomics Consortium (SGC)
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Amino-terminal Dimerization, NRDP1-Rhodanese Interaction, and Inhibited Catalytic Domain Conformation of the Ubiquitin-specific Protease 8 (USP8).
J.BIOL.CHEM. vol:281, pag:38061-38070 (2006) [PubMed ID 17035239 ]
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Hydrolase, Protease, Thiol protease, Ubl conjugation pathway, Deubiquitinating Enzyme, DUB, Zinc ribbon, Structural Genomics Consortium, SGC
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3.1.2.15 ExPASy BRENDA (A)
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Homo sapiens(human) 9606(A)
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Ubiquitin carboxyl-terminal hydrolase 8 (EC 3.1.2.15) (Ubiquitin thioesterase 8) (Ubiquitin-specific-processing protease 8) (Deubiquitinating enzyme 8) (hUBPy) P40818 (A)
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A
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2a9u, 1whb, 2fzp
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Ubiquitin carboxyl-terminal hydrolase 8 |
Protein |
P40818 (UBP8_HUMAN)
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396 |
85% |
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| A |
ZINC ION |
ZN
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