Research workbench
Nucleotide-dependent conformational changes in a protease-associated ATPase hslu
Analyse Nucleotide-dependent conformational changes in a protease-associated ATPase hslu in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HT2
- Type
- protein
- Length
- 3,024 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Heat shock locus hslv; Heat shock locus hslu
- UniProt
- P0A7B8, P0A6H5
- Ligands
- ADP
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 2 distinct chains · 48% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, I, J, K, L | Heat shock locus hslv | protein | 174 | 34% helix, 29% strand | P0A7B8 |
| E, F, G, H | Heat shock locus hslu | protein | 408 | 54% helix, 10% strand | P0A6H5 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 4 copies · chains E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 964 | 0.87 | 0.88 | 98 | ADP |
| 2 | 1086 | 0.86 | 0.87 | 98 | ADP |
| 3 | 609 | 0.68 | 0.77 | 70 | empty |
| 4 | 629 | 0.68 | 0.77 | 73 | empty |
| 5 | 519 | 0.66 | 0.77 | 63 | empty |
Interfaces
10 interfaces between chains.
- G–H · 2528 Ų buried · 40 hydrogen bonds · protein-protein
- E–F · 2238 Ų buried · 19 hydrogen bonds · protein-protein
- K–L · 729 Ų buried · 9 hydrogen bonds · protein-protein
- I–J · 516 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 494 Ų buried · 4 hydrogen bonds · protein-protein
Compared structures
- 1HT2 · Nucleotide-Dependent Conformational Changes in a Protease-Associated ATPase HslU · the same entry in another collection · chain L against L, 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 P0A7B8
- Every structure of UniProt P0A6H5
- Elsewhere: RCSB PDB 1HT2 · PDBe 1HT2 · UniProt P0A7B8 · UniProt P0A6H5
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