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UniProt O55000

O55000

O55000 (UniProt O55000): 7 experimental structures on GenesisL1. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
O55000
Experimental structures
7
Predicted models
0

Structures

7 records of O55000 in the MolNFT archive: 7 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
4MOYStructure of a second nuclear PP1 Holoenzyme, crystal form 1x-ray diffractionB——
4MOYStructure of a second nuclear PP1 holoenzyme, crystal form 1x-ray diffractionB——
4MP0Structure of a second nuclear PP1 Holoenzyme, crystal form 2x-ray diffractionB, D——
4MP0Structure of a second nuclear PP1 holoenzyme, crystal form 2x-ray diffractionB, D——
6VTISolution NMR structure of the N-terminal domain of the SERINE/THREONINE-protein phosphatase 1…solution nmrA——
7LQTSolution NMR structure of the pnuts amino-terminal domain fused to myc homology box 0solution nmrA——
O55000AlphaFold monomer V2.0 prediction for SERINE/THREONINE-protein phosphatase 1 regulatory subunit 10…———

Elsewhere

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