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UniProt P40818

Ubiquitin carboxyl-terminal hydrolase 8 (P40818)

Ubiquitin carboxyl-terminal hydrolase 8 (UniProt P40818), EC 3.4.19.12: 14 experimental structures on GenesisL1, 1 ligand bound, 21 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
P40818
Protein
Ubiquitin carboxyl-terminal hydrolase 8
EC
3.4.19.12
Experimental structures
14
Predicted models
0
Ligands
1
Pockets
21 · 2 records with a druggable one

Structures

14 records of P40818 in the MolNFT archive: 14 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
1WHBSolution structure of the Rhodanese-like domain in human ubiquitin specific protease 8 (UBP8)solution nmrA——
1WHBSolution structure of the rhodanese-like domain in human ubiquitin specific protease 8 (UBP8)solution nmrA——
2A9UStructure of the N-terminal domain of Human Ubiquitin carboxyl-terminal hydrolase 8 (USP8)x-ray diffractionA, B——
2A9UStructure of the N-terminal domain of human ubiquitin carboxyl-terminal hydrolase 8 (USP8)x-ray diffractionA, B——
2GFOStructure of the Catalytic Domain of Human Ubiquitin Carboxyl-terminal Hydrolase 8x-ray diffractionA——
2GFOStructure of the catalytic domain of human ubiquitin carboxyl-terminal hydrolase 8x-ray diffractionA——
2GWFStructure of a USP8-NRDP1 complexx-ray diffractionA, C, E——
2GWFStructure of a USP8-NRDP1 complexx-ray diffractionA, C, E——
3N3KThe catalytic domain of USP8 in complex with a USP8 specific inhibitorx-ray diffractionA——
3N3KThe catalytic domain of USP8 in complex with a USP8 specific inhibitorx-ray diffractionA——
6F09Binary complex of 14-3-3 zeta with ubiquitin specific protease 8 (USP8) pSer718 peptidex-ray diffractionA, B, C, D—5 (best 0.74)
6F09Binary complex of 14-3-3 zeta with ubiquitin specific protease 8 (USP8) PSER718 peptidex-ray diffractionA, B, C, D——
8XPNThe Crystal Structure of USP8 from Biortus.x-ray diffractionA, B, CZN16 (best 0.80)
P40818AlphaFold monomer V2.0 prediction for ubiquitin carboxyl-terminal hydrolase 8 (P40818)———

Ligands

  • ZN · Zinc ion · in 1 record

Elsewhere

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