MolNFT v1 · #229051 · protein
AlphaFold monomer V2.0 prediction for mediator of RNA polymerase II transcription subunit 26 (O95402)
O95402: “AlphaFold monomer V2.0 prediction for mediator of RNA polymerase II transcription subunit 26 (O95402)”. MolNFT v1 #229051 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- O95402
- Type
- protein
- Length
- 600 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5c4adF1416281C09AE8eE1cbb80fF7e44cE86F97
- UniProt
- O95402
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 600 | — | O95402 |
Compared structures
- 6ZV3 · Tfiis N-terminal domain (tnd) from human MED26 · an experimental structure of the same protein · chain A against A, TM-score 0.14
- 6ZV3 · TFIIS N-terminal domain (TND) from human MED26 · an experimental structure of the same protein · chain A against A, TM-score 0.14
- 5ODD · Human MED26 N-terminal domain (1-92) · an experimental structure of the same protein · chain A against A, TM-score 0.13
- 7ENC · TFIID-based PIC-Mediator holo-complex in fully-assembled state (hPIC-MED) · an experimental structure of the same protein · chain A against z, TM-score 0.12
- 7ENA · TFIID-based PIC-Mediator holo-complex in pre-assembled state (pre-hPIC-MED) · an experimental structure of the same protein · chain A against z, TM-score 0.12
- 7EMF · Human Mediator (deletion of MED1-IDR) in a Tail-extended conformation · an experimental structure of the same protein · chain A against Z, TM-score 0.12
- 7EMF · Human mediator (deletion of MED1-idr) in a tail-extended conformation · an experimental structure of the same protein · chain A against Z, TM-score 0.12
- 7ENJ · Human mediator (deletion of MED1-idr) in a tail-bent conformation (med-B) · an experimental structure of the same protein · chain A against Z, TM-score 0.12
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt O95402
- Elsewhere: UniProt O95402 · AlphaFold DB O95402
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