UniProt P32780
General transcription factor IIH subunit 1 (P32780)
General transcription factor IIH subunit 1 (UniProt P32780): 30 experimental structures on GenesisL1, 1 ligand bound, 4 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.
- UniProt
- P32780
- Protein
- General transcription factor IIH subunit 1
- Experimental structures
- 30
- Predicted models
- 0
- Ligands
- 1
- Pockets
- 4 · 1 record with a druggable one
Structures
30 records of P32780 in the MolNFT archive: 30 experimental, 0 predicted.
| Entry | Title | Method | Chains | Ligands | Pockets |
|---|---|---|---|---|---|
| 1PFJ | Solution structure of the N-terminal PH/PTB domain of the TFIIH P62 subunit | solution nmr | A | — | — |
| 1PFJ | Solution structure of the N-terminal PH/PTB domain of the tfiih P62 subunit | solution nmr | A | — | — |
| 2DII | Solution structure of the BSD domain of human TFIIH basal transcription factor complex p62 subunit | solution nmr | A | — | — |
| 2DII | Solution structure of the bsd domain of human tfiih basal transcription factor complex P62 subunit | solution nmr | A | — | — |
| 2RNR | Solution structure of the complex between TFIIE alpha C-terminal acidic domain and TFIIH p62 PH… | solution nmr | B | — | — |
| 2RNR | Solution structure of the complex between tfiie alpha C-terminal acidic domain and tfiih P62 pH… | solution nmr | B | — | — |
| 2RUK | Solution structure of the complex between p53 transactivation domain 2 and TFIIH p62 PH domain | solution nmr | B | — | — |
| 2RUK | Solution structure of the complex between P53 transactivation domain 2 and tfiih P62 pH domain | solution nmr | B | — | — |
| 2RVB | Solution structure of the complex between XPC acidic domain and TFIIH p62 PH domain | solution nmr | B | — | — |
| 2RVB | Solution structure of the complex between xpc acidic domain and tfiih P62 pH domain | solution nmr | B | — | — |
| 5GOW | Solution structure of the complex between DP1 acidic region and TFIIH p62 PH domain | solution nmr | B | — | — |
| 5GOW | Solution structure of the complex between DP1 acidic region and tfiih P62 pH domain | solution nmr | B | — | — |
| 5XV8 | Solution structure of the complex between uvssa acidic region and tfiih P62 pH domain | solution nmr | B | — | — |
| 6O9L | Human holo-pic in the closed state | electron microscopy | 1 | ZN | — |
| 6O9M | Structure of the human apo tfiih | electron microscopy | 1 | ZN | — |
| 7AD8 | Core tfiih-xpa-DNA complex with modelled P62 subunit | electron microscopy | I | — | — |
| 7BUL | Solution structure of the tandem pH and BSD1 domains of tfiih P62 | solution nmr | A | — | — |
| 7EGC | p53-bound TFIID-based holo PIC on HDM2 promoter | electron microscopy | 1 | — | — |
| 7ENA | TFIID-based PIC-Mediator holo-complex in pre-assembled state (pre-hPIC-MED) | electron microscopy | 1 | ZN | — |
| 7ENC | TFIID-based PIC-Mediator holo-complex in fully-assembled state (hPIC-MED) | electron microscopy | 1 | — | — |
| 7NVR | Human Mediator with RNA Polymerase II Pre-initiation complex | electron microscopy | 1 | — | — |
| 7NVR | Human mediator with RNA polymerase II pre-initiation complex | electron microscopy | 1 | — | — |
| 7NVW | Tfiih in a pre-translocated state (without ADP-BEF3) | electron microscopy | 1 | — | — |
| 7NVX | Tfiih in a post-translocated state (with ADP-BEF3) | electron microscopy | 1 | — | — |
| 7NVY | RNA polymerase II pre-initiation complex with closed promoter DNA in proximal position | electron microscopy | 1 | — | — |
| 7NVZ | RNA polymerase II pre-initiation complex with closed promoter DNA in distal position | electron microscopy | 1 | — | — |
| 7NW0 | RNA polymerase II pre-initiation complex with open promoter DNA | electron microscopy | 1 | — | — |
| 8EBU | XPC release from Core7-XPA-DNA (Cy5) | electron microscopy | C | — | — |
| 8EBW | Initial DNA-lesion (AP) binding by XPC and TFIIH complex2 | electron microscopy | C | — | 4 (best 0.73) |
| P32780 | AlphaFold monomer V2.0 prediction for general transcription factor iih subunit 1 (P32780) | — | — | — |
Ligands
- ZN · Zinc ion · in 3 records
Elsewhere
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