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UniProt P02941

P02941

P02941 (UniProt P02941): 15 experimental structures on GenesisL1. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
P02941
Experimental structures
15
Predicted models
0

Structures

15 records of P02941 in the MolNFT archive: 15 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
1JMWPropagating Conformational Changes Over Long (And Short) Distancesx-ray diffractionA——
1JMWPropagating conformational changes over long (and short) distancesx-ray diffractionA——
1LIHThree-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with…x-ray diffractionA——
1LIHThree-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with…x-ray diffractionA——
1VLSLigand binding domain of the wild-type aspartate receptorx-ray diffractionA——
1VLSLigand binding domain of the wild-type aspartate receptorx-ray diffractionA——
1VLTLigand binding domain of the wild-type aspartate receptor with aspartatex-ray diffractionA, B——
1VLTLigand binding domain of the wild-type aspartate receptor with aspartatex-ray diffractionA, B——
1WASThe three-dimensional structure of the ligand-binding domain of a wild-type bacterial chemotaxis…x-ray diffractionA——
1WASThe three-dimensional structure of the ligand-binding domain of a wild-type bacterial chemotaxis…x-ray diffractionA——
1WATThe three-dimensional structure of the ligand-binding domain of a wild-type bacterial chemotaxis…x-ray diffractionA, B——
1WATThe three-dimensional structure of the ligand-binding domain of a wild-type bacterial chemotaxis…x-ray diffractionA, B——
2LIGThree-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with…x-ray diffractionA, B——
2LIGThree-dimensional structures of the ligand-binding domain of the bacterial aspartate receptor with…x-ray diffractionA, B——
P02941AlphaFold monomer V2.0 prediction for methyl-accepting chemotaxis protein II (P02941)———

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