MolNFT v1 · #17002 · protein
Asymmetric complex between hslv and I-domain deleted hslu (H. influenzae)
1OFI · ATP-dependent hsl protease ATP-binding subunit hslu: “Asymmetric complex between hslv and I-domain deleted hslu (H. influenzae)”. X-ray diffraction, 4 ligands (ADP, LVS, MG), 20 pockets (best druggability 0.84). MolNFT v1 #17002 on…
- PDB
- 1OFI
- Type
- protein
- Length
- 1,928 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, LVS, MG, PO4
- Pockets
- 20 · best druggability 0.84
Structure
x-ray diffraction · 4 distinct chains · 47% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent hsl protease ATP-binding subunit hslu | protein | 299 | 51% helix, 13% strand | P43773 |
| B | ATP-dependent hsl protease ATP-binding subunit hslu | protein | 295 | 51% helix, 13% strand | P43773 |
| C | ATP-dependent hsl protease ATP-binding subunit hslu | protein | 296 | 48% helix, 10% strand | P43773 |
| G, H, I, L, M, N | ATP-dependent protease hslv (EC 3.4.25.-) | protein | 173 | 34% helix, 32% strand | P43772 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 3 copies · chains A, B, C
- LVS · 4-iodo-3-nitrophenyl acetyl-leucinyl-leucinyl-leucinyl-vinylsulfone · ligand · 3 copies · chains G, H, B, I
- 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, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 771 | 0.84 | 0.88 | 78 | ADP, MG, PO4 |
| 2 | 478 | 0.76 | 0.84 | 61 | empty |
| 3 | 549 | 0.66 | 0.77 | 57 | ADP, MG, PO4 |
| 4 | 141 | 0.64 | 0.87 | 23 | empty |
| 5 | 356 | 0.64 | 0.79 | 44 | MG |
Interfaces
11 interfaces between chains.
- B–C · 1643 Ų buried · 16 hydrogen bonds · protein-protein
- M–N · 665 Ų buried · 4 hydrogen bonds · protein-protein
- H–N · 654 Ų buried · 1 hydrogen bond · protein-protein
- B–H · 639 Ų buried · 5 hydrogen bonds · protein-protein
- H–I · 625 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 covalent (covalent ligand).
Compared structures
- 1OFI · 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 B against A, TM-score 0.96
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 1OFI · PDBe 1OFI · UniProt P43773 · UniProt P43772
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