Research workbench
Alpha-lytic protease at 120 K (single structure model)
Analyse Alpha-lytic protease at 120 K (single structure model) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TAL
- Type
- protein
- Length
- 198 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-lytic protease
- EC
- 3.4.21.12
- UniProt
- P00778
- Ligands
- TAM, SO4
- Pockets
- 1 · best druggability 0.29
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-lytic protease (EC 3.4.21.12) | protein | 198 | 7% helix, 55% strand | P00778 |
Ligands and binding sites
- TAM · Tris(hydroxyethyl)aminomethane · ligand · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
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 | 53 | 0.29 | 0.75 | 17 | SO4, TAM |
Modifications
Observed in the structure: 3 disulfide (disulfide).
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 P00778
- Elsewhere: RCSB PDB 1TAL · PDBe 1TAL · UniProt P00778
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