MolNFT v1 · #155024 · protein
Active conformation of hslv from staphylococcus aureus.
6KUI · ATP-dependent protease subunit hslv: “Active conformation of hslv from staphylococcus aureus.”. X-ray diffraction, 5 pockets (best druggability 0.64). MolNFT v1 #155024 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6KUI
- Type
- protein
- Length
- 518 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent protease subunit hslv
- EC
- 3.4.25.2
- UniProt
- P65796
- Pockets
- 5 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent protease subunit hslv (EC 3.4.25.2) | protein | 172 | 34% helix, 30% strand | P65796 |
| B, C | ATP-dependent protease subunit hslv (EC 3.4.25.2) | protein | 173 | 35% helix, 28% strand | P65796 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 412 | 0.64 | 0.78 | 41 | empty |
| 2 | 311 | 0.56 | 0.76 | 41 | empty |
| 3 | 180 | 0.52 | 0.79 | 23 | empty |
| 4 | 184 | 0.48 | 0.76 | 28 | empty |
| 5 | 56 | 0.26 | 0.73 | 17 | empty |
Interfaces
3 interfaces between chains.
- A–C · 817 Ų buried · 14 hydrogen bonds · protein-protein
- B–C · 742 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 515 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 6KUI · Active conformation of HslV from Staphylococcus aureus. · the same entry in another collection · chain A against A, TM-score 1.00
- P65796 · AlphaFold monomer V2.0 prediction for ATP-dependent protease subunit hslv (P65796) · 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 P65796
- Elsewhere: RCSB PDB 6KUI · PDBe 6KUI · UniProt P65796
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