Research workbench
3.74 ångströms resolution structure of hlsu with an axial-channel plug
Analyse 3.74 ångströms resolution structure of hlsu with an axial-channel plug in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PXL
- Type
- protein
- Length
- 4,667 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent protease ATPase subunit hslu
- UniProt
- C3SIX7
- Ligands
- ADP, MG, SO4
- Pockets
- 20 · best druggability 0.89
Structure
x-ray diffraction · 12 distinct chains · 59% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ATP-dependent protease ATPase subunit hslu | protein | 369 | 62% helix, 11% strand | C3SIX7 |
| B | ATP-dependent protease ATPase subunit hslu | protein | 417 | 59% helix, 12% strand | C3SIX7 |
| C | ATP-dependent protease ATPase subunit hslu | protein | 389 | 60% helix, 12% strand | C3SIX7 |
| D | ATP-dependent protease ATPase subunit hslu | protein | 401 | 62% helix, 10% strand | C3SIX7 |
| E | ATP-dependent protease ATPase subunit hslu | protein | 335 | 59% helix, 12% strand | C3SIX7 |
| F | ATP-dependent protease ATPase subunit hslu | protein | 410 | 60% helix, 12% strand | C3SIX7 |
| G | ATP-dependent protease ATPase subunit hslu | protein | 419 | 58% helix, 13% strand | C3SIX7 |
| H | ATP-dependent protease ATPase subunit hslu | protein | 395 | 59% helix, 13% strand | C3SIX7 |
| I | ATP-dependent protease ATPase subunit hslu | protein | 376 | 60% helix, 11% strand | C3SIX7 |
| J | ATP-dependent protease ATPase subunit hslu | protein | 331 | 58% helix, 12% strand | C3SIX7 |
| K | ATP-dependent protease ATPase subunit hslu | protein | 429 | 59% helix, 13% strand | C3SIX7 |
| L | ATP-dependent protease ATPase subunit hslu | protein | 396 | 59% helix, 12% strand | C3SIX7 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 12 copies · chains A, B, C, D, E, F, G, H, I, J, K, L
- MG · Magnesium ion · metal · 3 copies · chains A, F, H, I, K, L
- SO4 · Sulfate ion · ion · 2 copies · chains A, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 1158 | 0.89 | 0.91 | 145 | ADP, MG |
| 2 | 1189 | 0.89 | 0.90 | 147 | ADP |
| 3 | 814 | 0.88 | 0.91 | 98 | ADP |
| 4 | 817 | 0.88 | 0.91 | 104 | ADP |
| 5 | 605 | 0.86 | 0.91 | 68 | ADP |
Interfaces
21 interfaces between chains.
- A–F · 2830 Ų buried · 27 hydrogen bonds · protein-protein
- K–L · 2753 Ų buried · 24 hydrogen bonds · protein-protein
- G–H · 2657 Ų buried · 30 hydrogen bonds · protein-protein
- C–D · 2518 Ų buried · 26 hydrogen bonds · protein-protein
- H–I · 2410 Ų buried · 25 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 122 modified (engineered).
Compared structures
- 6PXL · 3.74 Angstroms resolution structure of HlsU with an axial-channel plug · the same entry in another collection · chain A against A, 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 C3SIX7
- Elsewhere: RCSB PDB 6PXL · PDBe 6PXL · UniProt C3SIX7
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