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UniProt Q56237

Chaperone protein DnaJ 2 (Q56237)

Chaperone protein DnaJ 2 (UniProt Q56237), EC 3.1.3.1: 15 experimental structures and 1 predicted model on GenesisL1, 16 pockets. Binding sites, druggability and experiment against prediction (TM-score) in GL1X.

UniProt
Q56237
Protein
Chaperone protein DnaJ 2
EC
3.1.3.1
Experimental structures
15
Predicted models
1
Pockets
16 · 1 record with a druggable one

Structures

16 records of Q56237 in the MolNFT archive: 15 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
4J7ZThermus thermophilus DNAJ J- and G/F-DOMAINSx-ray diffraction, eprA, B, C, D, E, F——
4J7ZThermus thermophilus dnaj J- and G/F-domainsx-ray diffraction; eprA, B, C, D, E, F——
4J80Thermus thermophilus DnaJx-ray diffraction, eprA, B, C, D——
4J80Thermus thermophilus dnajx-ray diffraction; eprA, B, C, D——
6PPTStructural basis for client recognition and activity of HSP40 chaperonessolution nmrA——
6PQEStructural Basis for Client Recognition and Activity of Hsp40 Chaperonessolution nmrA——
6PQEStructural basis for client recognition and activity of HSP40 chaperonessolution nmrA——
6PQMStructural Basis for Client Recognition and Activity of Hsp40 Chaperonessolution nmrA——
6PQMStructural basis for client recognition and activity of HSP40 chaperonessolution nmrA——
6PRIStructural basis for client recognition and activity of HSP40 chaperonessolution nmrA——
6PRJStructural basis for client recognition and activity of HSP40 chaperonessolution nmrA——
6PRPStructural basis for client recognition and activity of HSP40 chaperonessolution nmrA——
6PRQStructural basis for client recognition and activity of HSP40 chaperonessolution nmrA——
6PSIStructural Basis for Client Recognition and Activity of Hsp40 Chaperonessolution nmrA, C—16 (best 0.84)
6PSIStructural basis for client recognition and activity of HSP40 chaperonessolution nmrA, C——
Q56237AlphaFold monomer V2.0 prediction for chaperone protein dnaj 2 (Q56237)predictedA——

Experiment against prediction

Elsewhere

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