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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
- 1Z0G
- Type
- protein
- Length
- 1,174 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
- 19 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 35% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E | Putative protease la homolog type (EC 3.4.21.53) | protein | 195 | 36% helix, 29% strand | O29883 |
| B, C, D, F | Putative protease la homolog type (EC 3.4.21.53) | protein | 196 | 33% helix, 28% strand | O29883 |
Pockets
19 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 426 | 0.68 | 0.80 | 46 | empty |
| 2 | 402 | 0.68 | 0.80 | 55 | empty |
| 3 | 339 | 0.62 | 0.79 | 53 | empty |
| 4 | 106 | 0.59 | 0.86 | 26 | empty |
| 5 | 87 | 0.59 | 0.87 | 20 | empty |
Interfaces
6 interfaces between chains.
- D–E · 953 Ų buried · 14 hydrogen bonds · protein-protein
- C–D · 941 Ų buried · 17 hydrogen bonds · protein-protein
- A–F · 920 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 918 Ų buried · 14 hydrogen bonds · protein-protein
- B–C · 870 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 1Z0G · PDBe 1Z0G · UniProt O29883
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