MolNFT v1 · #151132 · protein
Crystal structure of escherichia COLI DEAH/RHA helicase hrpb
6HEG · ATP-dependent RNA helicase hrpb: “Crystal structure of escherichia COLI DEAH/RHA helicase hrpb”. X-ray diffraction, 3 ligands (ADP, ALF, PO4), 9 pockets (best druggability 0.80). MolNFT v1 #151132 on GenesisL1: 3D structure, binding…
- PDB
- 6HEG
- Type
- protein
- Length
- 783 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent RNA helicase hrpb
- EC
- 3.6.4.13
- UniProt
- P37024
- Ligands
- ADP, ALF, PO4
- Pockets
- 9 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent RNA helicase hrpb (EC 3.6.4.13) | protein | 783 | 34% helix, 20% strand | P37024 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- ALF · Tetrafluoroaluminate ion · ligand · chains A
- PO4 · Phosphate ion · ion · 6 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1070 | 0.80 | 0.81 | 91 | empty |
| 2 | 123 | 0.53 | 0.82 | 23 | empty |
| 3 | 109 | 0.49 | 0.81 | 22 | empty |
| 4 | 118 | 0.47 | 0.79 | 20 | ADP, ALF |
| 5 | 131 | 0.42 | 0.76 | 20 | empty |
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 6HEG · Crystal structure of Escherichia coli DEAH/RHA helicase HrpB · the same entry in another collection · chain A against A, TM-score 1.00
- P37024 · AlphaFold monomer V2.0 prediction for ATP-dependent RNA helicase hrpb (P37024) · a predicted model of the same protein · chain A against A, TM-score 0.90
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 P37024
- Elsewhere: RCSB PDB 6HEG · PDBe 6HEG · UniProt P37024
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