MolNFT v1 · #11345 · protein
Structure of haemophilus influenzae hslv protein at 1.9 a resolution
1JJW · ATP-dependent protease hslv: “Structure of haemophilus influenzae hslv protein at 1.9 a resolution”. X-ray diffraction, 1 ligand (K), 3 pockets (best druggability 0.71). MolNFT v1 #11345 on GenesisL1: 3D structure, binding sites and…
- PDB
- 1JJW
- Type
- protein
- Length
- 519 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent protease hslv
- EC
- 3.4.99.-
- UniProt
- P43772
- Ligands
- K
- Pockets
- 3 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | ATP-dependent protease hslv (EC 3.4.99.-) | protein | 173 | 36% helix, 29% strand | P43772 |
Ligands and binding sites
- K · Potassium ion · metal · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 761 | 0.71 | 0.78 | 64 | empty |
| 2 | 328 | 0.63 | 0.79 | 46 | empty |
| 3 | 64 | 0.50 | 0.85 | 21 | empty |
Interfaces
2 interfaces between chains.
- A–B · 856 Ų buried · 19 hydrogen bonds · protein-protein
- A–C · 378 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1JJW · Structure of Haemophilus influenzae HslV Protein at 1.9 A Resolution · the same entry in another collection · chain A against A, TM-score 1.00
- P43772 · AlphaFold monomer V2.0 prediction for ATP-dependent protease subunit hslv (P43772) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 P43772
- Elsewhere: RCSB PDB 1JJW · PDBe 1JJW · UniProt P43772
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