Research workbench
Crystal structure of the hsluv protease-chaperone complex
Analyse Crystal structure of the hsluv protease-chaperone complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1G3I
- Type
- protein
- Length
- 5,919 residues
- Chains
- 24
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ATP-dependent hslu protease ATP-binding subunit hslu; ATP-dependent protease hslv
- EC
- 3.4.99.-
- UniProt
- P43773, P43772
- Ligands
- ATP
- Pockets
- 20 · best druggability 0.85
Structure
x-ray diffraction · 12 distinct chains · 42% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | ATP-dependent hslu protease ATP-binding subunit hslu | protein | 326 | 51% helix, 12% strand | P43773 |
| C | ATP-dependent hslu protease ATP-binding subunit hslu | protein | 319 | 52% helix, 13% strand | P43773 |
| D | ATP-dependent hslu protease ATP-binding subunit hslu | protein | 318 | 53% helix, 13% strand | P43773 |
| E | ATP-dependent hslu protease ATP-binding subunit hslu | protein | 317 | 53% helix, 13% strand | P43773 |
| F | ATP-dependent hslu protease ATP-binding subunit hslu | protein | 320 | 52% helix, 13% strand | P43773 |
| G, H, I, J, K, L, M, N, O, P, Q, R | ATP-dependent protease hslv (EC 3.4.99.-) | protein | 173 | 30% helix, 32% strand | P43772 |
| S | ATP-dependent hslu protease ATP-binding subunit hslu | protein | 317 | 34% helix, 13% strand | P43773 |
| T | ATP-dependent hslu protease ATP-binding subunit hslu | protein | 331 | 34% helix, 12% strand | P43773 |
| U | ATP-dependent hslu protease ATP-binding subunit hslu | protein | 322 | 35% helix, 12% strand | P43773 |
| V | ATP-dependent hslu protease ATP-binding subunit hslu | protein | 313 | 35% helix, 13% strand | P43773 |
| W | ATP-dependent hslu protease ATP-binding subunit hslu | protein | 312 | 33% helix, 13% strand | P43773 |
| X | ATP-dependent hslu protease ATP-binding subunit hslu | protein | 322 | 33% helix, 12% strand | P43773 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · 12 copies · chains A, B, C, D, E, F, S, X, T, U, V, W
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 | 934 | 0.85 | 0.86 | 87 | ATP |
| 2 | 1181 | 0.85 | 0.86 | 113 | ATP |
| 3 | 977 | 0.84 | 0.85 | 89 | ATP |
| 4 | 860 | 0.84 | 0.86 | 88 | ATP |
| 5 | 1054 | 0.84 | 0.85 | 86 | ATP |
Interfaces
72 interfaces between chains.
- S–X · 1703 Ų buried · 19 hydrogen bonds · protein-protein
- T–U · 1696 Ų buried · 18 hydrogen bonds · protein-protein
- U–V · 1696 Ų buried · 15 hydrogen bonds · protein-protein
- W–X · 1692 Ų buried · 19 hydrogen bonds · protein-protein
- S–T · 1664 Ų buried · 16 hydrogen bonds · protein-protein
Compared structures
- 1G3I · Crystal structure of the hsluv protease-chaperone complex · the same entry in another collection · chain K against K, 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 P43773
- Every structure of UniProt P43772
- Elsewhere: RCSB PDB 1G3I · PDBe 1G3I · UniProt P43773 · UniProt P43772
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