Research workbench
Hslu L199Q in hsluv complex
Analyse Hslu L199Q in hsluv complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5JI2
- Type
- protein
- Length
- 1,424 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent protease subunit hslv; ATP-dependent protease ATPase subunit hslu
- EC
- 3.4.25.2
- UniProt
- B7LA29, P0A6H6
- Ligands
- ADP, MG
- Pockets
- 14 · best druggability 0.87
Structure
x-ray diffraction · 3 distinct chains · 55% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | ATP-dependent protease subunit hslv (EC 3.4.25.2) | protein | 174 | 39% helix, 30% strand | B7LA29 |
| E | ATP-dependent protease ATPase subunit hslu | protein | 375 | 61% helix, 9% strand | P0A6H6 |
| F | ATP-dependent protease ATPase subunit hslu | protein | 353 | 58% helix, 11% strand | P0A6H6 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains E, F
- MG · Magnesium ion · metal · 3 copies · chains A, B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1056 | 0.87 | 0.89 | 119 | ADP |
| 2 | 97 | 0.78 | 0.98 | 23 | empty |
| 3 | 104 | 0.78 | 0.97 | 24 | empty |
| 4 | 904 | 0.74 | 0.77 | 92 | MG |
| 5 | 265 | 0.67 | 0.83 | 41 | empty |
Interfaces
9 interfaces between chains.
- E–F · 2174 Ų buried · 23 hydrogen bonds · protein-protein
- C–D · 745 Ų buried · 9 hydrogen bonds · protein-protein
- A–D · 644 Ų buried · 2 hydrogen bonds · protein-protein
- B–C · 620 Ų buried · 0 hydrogen bonds · protein-protein
- B–D · 474 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 5JI2 · HslU L199Q in HslUV complex · the same entry in another collection · chain F against F, TM-score 1.00
- B7LA29 · AlphaFold monomer V2.0 prediction for ATP-dependent protease subunit hslv (B7LA29) · a predicted model of the same protein · chain A against A, TM-score 0.98
- P0A6H6 · AlphaFold monomer V2.0 prediction for ATP-dependent protease ATPase subunit hslu (P0A6H6) · a predicted model of the same protein · chain F against A, TM-score 0.97
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 B7LA29
- Every structure of UniProt P0A6H6
- Elsewhere: RCSB PDB 5JI2 · PDBe 5JI2 · UniProt B7LA29 · UniProt P0A6H6
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