Research workbench
Solution structure of RTT103 ctd-interacting domain bound to a THR4 phosphorylated ctd peptide
Analyse Solution structure of RTT103 ctd-interacting domain bound to a THR4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LVF
- Type
- protein
- Length
- 158 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Regulator of TY1 transposition protein 103; Pro-ser-tyr-ser-pro-pth-ser-pro-ser-tyr-ser-pr…
- UniProt
- Q05543
- Pockets
- 2 · best druggability 0.35
Structure
solution nmr · 2 distinct chains · 65% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Regulator of TY1 transposition protein 103 | protein | 142 | 73% helix, 0% strand | Q05543 |
| B | Pro-ser-tyr-ser-pro-pth-ser-pro-ser-tyr-ser-pro-thr-ser- pro-ser | protein | 16 | 0% helix, 0% strand | — |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 102 | 0.35 | 0.74 | 17 | empty |
| 2 | 68 | 0.32 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 798 Ų buried · 22 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 5LVF · Solution structure of Rtt103 CTD-interacting domain bound to a Thr4 phosphorylated CTD… · the same entry in another collection · chain A against A, TM-score 1.00
- Q05543 · AlphaFold monomer V2.0 prediction for regulator of TY1 transposition protein 103 (Q05543) · a predicted model of the same protein · chain A against A, TM-score 0.91
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 Q05543
- Elsewhere: RCSB PDB 5LVF · PDBe 5LVF · UniProt Q05543
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