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Crystal structure of a. fulgidus lon proteolytic domain
Analyse Crystal structure of a. fulgidus lon proteolytic domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Z0E
- Type
- protein
- Length
- 1,169 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative protease la homolog type
- EC
- 3.4.21.53
- UniProt
- O29883
- Pockets
- 20 · best druggability 0.67
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, D, E, F | Putative protease la homolog type (EC 3.4.21.53) | protein | 195 | 35% helix, 29% strand | O29883 |
| C | Putative protease la homolog type (EC 3.4.21.53) | protein | 194 | 34% helix, 30% strand | O29883 |
Pockets
20 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 348 | 0.67 | 0.81 | 42 | empty |
| 2 | 323 | 0.65 | 0.80 | 37 | empty |
| 3 | 72 | 0.62 | 0.91 | 20 | empty |
| 4 | 104 | 0.60 | 0.87 | 25 | empty |
| 5 | 254 | 0.56 | 0.77 | 39 | empty |
Interfaces
6 interfaces between chains.
- A–F · 914 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 892 Ų buried · 17 hydrogen bonds · protein-protein
- D–E · 881 Ų buried · 19 hydrogen bonds · protein-protein
- C–D · 873 Ų buried · 7 hydrogen bonds · protein-protein
- E–F · 854 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
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 O29883
- Elsewhere: RCSB PDB 1Z0E · PDBe 1Z0E · UniProt O29883
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