MolNFT v1 · #27365 · protein
Crystal structure of M. jannaschii lon proteolytic domain
1XHK · Putative protease la homolog: “Crystal structure of M. jannaschii lon proteolytic domain”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.68). MolNFT v1 #27365 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 1XHK
- Type
- protein
- Length
- 372 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative protease la homolog
- EC
- 3.4.21.-
- UniProt
- Q58812
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative protease la homolog (EC 3.4.21.-) | protein | 185 | 33% helix, 28% strand | Q58812 |
| B | Putative protease la homolog (EC 3.4.21.-) | protein | 187 | 32% helix, 29% strand | Q58812 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 3 copies · chains A, B
- MES · 2-(N-morpholino)-ethanesulfonic acid · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 394 | 0.68 | 0.81 | 64 | empty |
Interfaces
1 interface between chains.
- A–B · 701 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 modified (engineered).
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 Q58812
- Elsewhere: RCSB PDB 1XHK · PDBe 1XHK · UniProt Q58812
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