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UniProt P05387

P05387

P05387 (UniProt P05387): 11 experimental structures on GenesisL1. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
P05387
Experimental structures
11
Predicted models
0

Structures

11 records of P05387 in the MolNFT archive: 11 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
1S4JNMR structure of cross-reactive peptides from Homo sapienssolution nmrA——
1S4JNMR structure of cross-reactive peptides from homo sapienssolution nmrA——
2LBFSolution structure of the dimerization domain of human ribosomal protein P1/P2 heterodimersolution nmrB——
2LBFSolution structure of the dimerization domain of human ribosomal protein P1/P2 heterodimersolution nmrB——
2W1ONMR structure of dimerization domain of human ribosomal protein P2solution nmrA, B——
2W1ONMR structure of dimerization domain of human ribosomal protein P2solution nmrA, B——
4BEHSolution structure of human ribosomal protein P1.P2 heterodimersolution nmrB——
4BEHSolution structure of human ribosomal protein P1.P2 heterodimersolution nmrB——
4V6XStructure of the human 80S ribosomeelectron microscopyCu, Cv——
5DDZCrystal structure of the rta-C10-P2 complexx-ray diffractionB——
P05387AlphaFold monomer V2.0 prediction for 60S acidic ribosomal protein P2 (P05387)———

Elsewhere

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