MolNFT v1 · #16489 · protein
1.9 ångström crystal structure of a plant cysteine protease ervatamin C
1O0E: “1.9 ångström crystal structure of a plant cysteine protease ervatamin C”. X-ray diffraction, 1 ligand (THJ), 1 pocket (best druggability 0.75). MolNFT v1 #16489 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1O0E
- Type
- protein
- Length
- 416 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ervatamin C
- UniProt
- P83654
- Ligands
- THJ
- Pockets
- 1 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 27% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ervatamin C | protein | 208 | 27% helix, 21% strand | P83654 |
Ligands and binding sites
- THJ · Thiosulfate · ligand · 2 copies · chains A, 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 | 749 | 0.75 | 0.80 | 80 | empty |
Interfaces
1 interface between chains.
- A–B · 615 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 disulfide, 2 covalent (disulfide, covalent ligand).
Compared structures
- 1O0E · 1.9 Angstrom Crystal Structure of a plant cysteine protease Ervatamin C · the same entry in another collection · 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 P83654
- Elsewhere: RCSB PDB 1O0E · PDBe 1O0E · UniProt P83654
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