Research workbench
Aqualysin I: the crystal structure of a serine protease from an extreme thermophile, thermus aquaticus yt-1
Analyse Aqualysin I: the crystal structure of a serine protease from an extreme… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DZT
- Type
- protein
- Length
- 276 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aqualysin-1
- EC
- 3.4.21.111
- UniProt
- P08594
- Ligands
- PMS, CA
- Pockets
- 1 · best druggability 0.35
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aqualysin-1 (EC 3.4.21.111) | protein | 276 | 28% helix, 23% strand | P08594 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 86 | 0.35 | 0.75 | 27 | PMS |
Modifications
Observed in the structure: 2 disulfide, 1 covalent (disulfide, covalent ligand).
Compared structures
- 4DZT · Aqualysin I: the crystal structure of a serine protease from an extreme thermophile… · the same entry in another collection · chain A against A, TM-score 1.00
- P08594 · AlphaFold monomer V2.0 prediction for aqualysin-1 (P08594) · a predicted model of the same protein · chain A against A, 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 P08594
- Elsewhere: RCSB PDB 4DZT · PDBe 4DZT · UniProt P08594
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