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UniProt P40485

P40485

P40485 (UniProt P40485): 11 experimental structures on GenesisL1. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
P40485
Experimental structures
11
Predicted models
0

Structures

11 records of P40485 in the MolNFT archive: 11 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
3NSUA Systematic Screen for Protein-Lipid Interactions in Saccharomyces cerevisiaex-ray diffractionA, B——
3NSUA systematic screen for protein-lipid interactions in saccharomyces cerevisiaex-ray diffractionA, B——
4A5KStructural analyses of Slm1-PH domain demonstrate ligand binding in the non-canonical sitex-ray diffractionA, B, C, D——
4A5KStructural analyses of SLM1-pH domain demonstrate ligand binding in the non-canonical sitex-ray diffractionA, B, C, D——
4A6FCrystal structure of Slm1-PH domain in complex with Phosphoserinex-ray diffractionA, B——
4A6FCrystal structure of SLM1-pH domain in complex with phosphoserinex-ray diffractionA, B——
4A6HCrystal structure of Slm1-PH domain in complex with Inositol-4- phosphatex-ray diffractionA, B, C, D——
4A6HCrystal structure of SLM1-pH domain in complex with inositol-4-phosphatex-ray diffractionA, B, C, D——
4A6KCrystal structure of Slm1-PH domain in complex with D-myo-Inositol-4- phosphatex-ray diffractionA, B, C, D——
4A6KCrystal structure of SLM1-pH domain in complex with D-myo-inositol-4-phosphatex-ray diffractionA, B, C, D——
P40485AlphaFold monomer V2.0 prediction for phosphatidylinositol 4,5-bisphosphate-binding protein SLM1…———

Elsewhere

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