MolNFT v1 · #17001 · protein
Asymmetric complex between hslv and I-domain deleted hslu (H. influenzae)
1OFH · ATP-dependent hsl protease ATP-binding subunit hslu: “Asymmetric complex between hslv and I-domain deleted hslu (H. influenzae)”. X-ray diffraction, 3 ligands (ADP, MG, PO4), 20 pockets (best druggability 0.82). MolNFT v1 #17001 on…
- PDB
- 1OFH
- Type
- protein
- Length
- 1,965 residues
- Chains
- 9
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent hsl protease ATP-binding subunit hslu; ATP-dependent protease hslv
- EC
- 3.4.25.-
- UniProt
- P43773, P43772
- Ligands
- ADP, MG, PO4
- Pockets
- 20 · best druggability 0.82
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | ATP-dependent hsl protease ATP-binding subunit hslu | protein | 309 | 50% helix, 13% strand | P43773 |
| G, H, I, L, M, N | ATP-dependent protease hslv (EC 3.4.25.-) | protein | 173 | 30% helix, 31% strand | P43772 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 3 copies · chains A, B, C
- MG · Magnesium ion · metal · 12 copies · chains A, B, C, G, H, I, L, M, N
- PO4 · Phosphate ion · ion · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 442 | 0.82 | 0.90 | 54 | ADP, MG, PO4 |
| 2 | 304 | 0.77 | 0.89 | 45 | empty |
| 3 | 186 | 0.73 | 0.90 | 42 | empty |
| 4 | 52 | 0.68 | 0.97 | 17 | empty |
| 5 | 530 | 0.67 | 0.77 | 61 | ADP, MG, PO4 |
Interfaces
12 interfaces between chains.
- B–C · 1810 Ų buried · 17 hydrogen bonds · protein-protein
- A–G · 692 Ų buried · 9 hydrogen bonds · protein-protein
- M–N · 670 Ų buried · 7 hydrogen bonds · protein-protein
- C–I · 653 Ų buried · 7 hydrogen bonds · protein-protein
- H–N · 653 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 1OFH · Asymmetric complex between HslV and I-domain deleted HslU (H. influenzae) · the same entry in another collection · chain N against N, TM-score 1.00
- P43773 · AlphaFold monomer V2.0 prediction for ATP-dependent protease ATPase subunit hslu (P43773) · a predicted model of the same protein · chain A against A, TM-score 0.95
- P43772 · AlphaFold monomer V2.0 prediction for ATP-dependent protease subunit hslv (P43772) · a predicted model of the same protein · chain G against A, TM-score 0.94
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 P43773
- Every structure of UniProt P43772
- Elsewhere: RCSB PDB 1OFH · PDBe 1OFH · UniProt P43773 · UniProt P43772
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.