Research workbench
Crystal structure of the hutp antitermination complex bound to a single stranded region of hut mRNA
Analyse Crystal structure of the hutp antitermination complex bound to a single… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1WPU
- Type
- protein + RNA
- Length
- 308 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5'-R(*UP*UP*GP*AP*GP*UP*U)-3'; Hut operon positive regulatory protein
- UniProt
- P10943
- Ligands
- HIS, MG
- Pockets
- 3 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, D | 5'-R(*UP*UP*GP*AP*GP*UP*U)-3' | rna | 7 | — | — |
| A, B | Hut operon positive regulatory protein | protein | 147 | 39% helix, 30% strand | P10943 |
Ligands and binding sites
- HIS · Histidine · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 123 | 0.46 | 0.79 | 22 | empty |
| 2 | 111 | 0.45 | 0.79 | 23 | empty |
| 3 | 53 | 0.22 | 0.71 | 16 | MG, HIS |
Interfaces
3 interfaces between chains.
- A–B · 1369 Ų buried · 22 hydrogen bonds · protein-protein
- D–B · 702 Ų buried · 21 hydrogen bonds · protein-nucleic
- C–A · 671 Ų buried · 17 hydrogen bonds · protein-nucleic
Compared structures
- 1WPU · Crystal Structure of the HutP antitermination complex bound to a single stranded region… · the same entry in another collection · chain C against C, TM-score 1.00
- P10943 · AlphaFold monomer V2.0 prediction for hut operon positive regulatory protein (P10943) · a predicted model of the same protein · chain A against A, TM-score 1.00
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 P10943
- Elsewhere: RCSB PDB 1WPU · PDBe 1WPU · UniProt P10943
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