Research workbench
Structural and functional insights into the human UPF1 helicase core
Analyse Structural and functional insights into the human UPF1 helicase core in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2GJK
- Type
- protein
- Length
- 614 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Regulator of nonsense transcripts 1
- EC
- 3.6.1.-
- UniProt
- Q92900
- Ligands
- ANP, MG
- Pockets
- 7 · best druggability 0.85
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Regulator of nonsense transcripts 1 (EC 3.6.1.-) | protein | 614 | 37% helix, 18% strand | Q92900 |
Ligands and binding sites
- ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1176 | 0.85 | 0.86 | 100 | empty |
| 2 | 155 | 0.61 | 0.85 | 32 | MG, ANP |
| 3 | 363 | 0.60 | 0.77 | 31 | empty |
| 4 | 109 | 0.42 | 0.76 | 15 | empty |
| 5 | 74 | 0.39 | 0.78 | 17 | empty |
Compared structures
- 2GJK · Structural and functional insights into the human Upf1 helicase core · the same entry in another collection · chain A against A, TM-score 1.00
- Q92900 · AlphaFold monomer V2.0 prediction for regulator of nonsense transcripts 1 (Q92900) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q92900
- Elsewhere: RCSB PDB 2GJK · PDBe 2GJK · UniProt Q92900
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