Research workbench
Structure and refinement of penicillopepsin at 1.8 ångströms resolution
Analyse Structure and refinement of penicillopepsin at 1.8 ångströms resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3APP
- Type
- protein
- Length
- 323 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Penicillopepsin
- EC
- 3.4.23.20
- UniProt
- P00798
- Pockets
- 1 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 14% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Penicillopepsin (EC 3.4.23.20) | protein | 323 | 14% helix, 48% strand | P00798 |
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 | 449 | 0.60 | 0.75 | 37 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 3APP · Structure and refinement of penicillopepsin at 1.8 ångströms resolution · the same entry in another collection · chain A against A, TM-score 1.00
- P00798 · AlphaFold monomer V2.0 prediction for penicillopepsin-1 (P00798) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P00798
- Elsewhere: RCSB PDB 3APP · PDBe 3APP · UniProt P00798
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.