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UniProt P51946

Cyclin-H (P51946)

Cyclin-H (UniProt P51946): 38 experimental structures and 1 predicted model on GenesisL1, 117 pockets. Binding sites, druggability and experiment against prediction (TM-score) in GL1X.

UniProt
P51946
Protein
Cyclin-H
Experimental structures
38
Predicted models
1
Pockets
117 · 22 records with a druggable one

Structures

39 records of P51946 in the MolNFT archive: 38 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
1JKWStructure of cyclin MCS2x-ray diffractionA——
1JKWStructure of cyclin MCS2x-ray diffractionA——
1KXUCyclin H, a positive regulatory subunit of cdk activating kinasex-ray diffractionA——
1KXUCyclin H, a positive regulatory subunit of cdk activating kinasex-ray diffractionA——
6O9LHuman holo-pic in the closed stateelectron microscopy9——
6XBZStructure of the human CDK-activating kinaseelectron microscopyI—7 (best 0.76)
6XBZStructure of the human cdk-activating kinaseelectron microscopyI——
6XD3Structure of the human CAK in complex with THZ1electron microscopyI——
6XD3Structure of the human cak in complex with THZ1electron microscopyI——
7B5OCryo-EM structure of the human cak bound to ICEC0942 at 2.5 ångströms resolutionelectron microscopyI——
7B5QCryo-EM structure of the human CAK bound to ICEC0942 (PHENIX-OPLS3e)electron microscopyI——
7B5QCryo-EM structure of the human cak bound to ICEC0942 (phenix-OPLS3E)electron microscopyI——
7EGBTFIID-based holo PIC on SCP promoterelectron microscopy9—1 (best 0.77)
7EGCp53-bound TFIID-based holo PIC on HDM2 promoterelectron microscopy9——
7ENATFIID-based PIC-Mediator holo-complex in pre-assembled state (pre-hPIC-MED)electron microscopy9——
7ENCTFIID-based PIC-Mediator holo-complex in fully-assembled state (hPIC-MED)electron microscopy9——
7NVRHuman Mediator with RNA Polymerase II Pre-initiation complexelectron microscopy9——
7NVRHuman mediator with RNA polymerase II pre-initiation complexelectron microscopy9——
8BVWRNA polymerase II pre-initiation complex with the distal +1 nucleosome (PIC-Nuc18W)electron microscopy9—1 (best 0.82)
8BYQRNA polymerase II pre-initiation complex with the proximal +1 nucleosome (PIC-Nuc10W)electron microscopy9—1 (best 0.78)
8GXQPIC-Mediator in complex with +1 nucleosome (T40N) in MH-binding stateelectron microscopyHJ—1 (best 0.82)
8ORMCryo-EM structure of CAK-THZ1electron microscopyI—7 (best 0.76)
8P6VCryo-EM structure of CAK in complex with inhibitor ICEC0942electron microscopyI—4 (best 0.73)
8P6WCryo-EM structure of CAK in complex with inhibitor BS-181electron microscopyI—5 (best 0.76)
8P6XCryo-EM structure of CAK in complex with inhibitor BS-194electron microscopyI—7 (best 0.75)
8P6ZCryo-EM structure of CAK in complex with inhibitor ICEC0510-Relectron microscopyI—6 (best 0.74)
8P70Cryo-EM structure of CAK in complex with inhibitor ICEC0510-Selectron microscopyI—6 (best 0.77)
8P71Cryo-EM structure of CAK in complex with inhibitor ICEC0574electron microscopyI—5 (best 0.76)
8P72Cryo-EM structure of CAK in complex with inhibitor ICEC0768electron microscopyI—5 (best 0.74)
8P73Cryo-EM structure of CAK in complex with inhibitor ICEC0829electron microscopyI—5 (best 0.77)
8P74Cryo-EM structure of CAK in complex with inhibitor ICEC0880 (ring-up conformation)electron microscopyI—5 (best 0.75)
8P75Cryo-EM structure of CAK in complex with inhibitor ICEC0880 (ring-down conformation)electron microscopyI—6 (best 0.76)
8P77Cryo-EM structure of CAK in complex with inhibitor ICEC0943electron microscopyI—5 (best 0.74)
8P78Cryo-EM structure of CAK in complex with inhibitor dinaciclibelectron microscopyI—6 (best 0.74)
8PLZCryo-EM structure of CAK in complex with inhibitor CT7030electron microscopyI—5 (best 0.74)
8PYRCrystal structure of the dual T-loop phosphorylated Cdk7/CycH/Mat1 complexx-ray diffractionB, F—17 (best 0.78)
8S0RCryo-EM structure of CAK modified by covalent inhibitor SY-1365electron microscopyI—7 (best 0.74)
8S0TCryo-EM structure of CAK in complex with SY-5609electron microscopyI—5 (best 0.71)
P51946AlphaFold monomer V2.0 prediction for cyclin-H (P51946)predictedA——

Experiment against prediction

Elsewhere

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