Research workbench
Hslu from staphylococcus aureus
Analyse Hslu from staphylococcus aureus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6KWW
- Type
- protein
- Length
- 7,336 residues
- Chains
- 24
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent protease ATPase subunit hslu
- UniProt
- P63796
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 24 distinct chains · 54% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| M | ATP-dependent protease ATPase subunit hslu | protein | 317 | 56% helix, 13% strand | P63796 |
| N | ATP-dependent protease ATPase subunit hslu | protein | 311 | 55% helix, 13% strand | P63796 |
| O | ATP-dependent protease ATPase subunit hslu | protein | 302 | 50% helix, 14% strand | P63796 |
| P | ATP-dependent protease ATPase subunit hslu | protein | 302 | 54% helix, 13% strand | P63796 |
| Q | ATP-dependent protease ATPase subunit hslu | protein | 303 | 54% helix, 13% strand | P63796 |
| R | ATP-dependent protease ATPase subunit hslu | protein | 330 | 57% helix, 13% strand | P63796 |
| S | ATP-dependent protease ATPase subunit hslu | protein | 309 | 55% helix, 12% strand | P63796 |
| T | ATP-dependent protease ATPase subunit hslu | protein | 330 | 53% helix, 12% strand | P63796 |
| U | ATP-dependent protease ATPase subunit hslu | protein | 332 | 54% helix, 12% strand | P63796 |
| V | ATP-dependent protease ATPase subunit hslu | protein | 301 | 55% helix, 13% strand | P63796 |
| W | ATP-dependent protease ATPase subunit hslu | protein | 323 | 60% helix, 13% strand | P63796 |
| X | ATP-dependent protease ATPase subunit hslu | protein | 316 | 56% helix, 13% strand | P63796 |
| A | ATP-dependent protease ATPase subunit hslu | protein | 307 | 53% helix, 14% strand | P63796 |
| B | ATP-dependent protease ATPase subunit hslu | protein | 292 | 51% helix, 14% strand | P63796 |
| C | ATP-dependent protease ATPase subunit hslu | protein | 296 | 56% helix, 14% strand | P63796 |
| D | ATP-dependent protease ATPase subunit hslu | protein | 296 | 50% helix, 14% strand | P63796 |
| E | ATP-dependent protease ATPase subunit hslu | protein | 292 | 51% helix, 13% strand | P63796 |
| F | ATP-dependent protease ATPase subunit hslu | protein | 298 | 56% helix, 14% strand | P63796 |
| G | ATP-dependent protease ATPase subunit hslu | protein | 287 | 49% helix, 14% strand | P63796 |
| H | ATP-dependent protease ATPase subunit hslu | protein | 304 | 54% helix, 13% strand | P63796 |
| I | ATP-dependent protease ATPase subunit hslu | protein | 291 | 52% helix, 14% strand | P63796 |
| J | ATP-dependent protease ATPase subunit hslu | protein | 305 | 53% helix, 12% strand | P63796 |
| K | ATP-dependent protease ATPase subunit hslu | protein | 297 | 53% helix, 13% strand | P63796 |
| L | ATP-dependent protease ATPase subunit hslu | protein | 295 | 51% helix, 12% strand | P63796 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 991 | 0.87 | 0.88 | 112 | empty |
| 2 | 923 | 0.86 | 0.88 | 100 | empty |
| 3 | 820 | 0.86 | 0.88 | 97 | empty |
| 4 | 898 | 0.86 | 0.87 | 92 | empty |
| 5 | 845 | 0.85 | 0.88 | 88 | empty |
Interfaces
67 interfaces between chains.
- T–U · 2283 Ų buried · 21 hydrogen bonds · protein-protein
- N–O · 2243 Ų buried · 18 hydrogen bonds · protein-protein
- D–E · 2176 Ų buried · 22 hydrogen bonds · protein-protein
- O–P · 2175 Ų buried · 18 hydrogen bonds · protein-protein
- V–W · 2138 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 6KWW · HslU from Staphylococcus aureus · the same entry in another collection · chain W against W, TM-score 1.00
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 P63796
- Elsewhere: RCSB PDB 6KWW · PDBe 6KWW · UniProt P63796
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