Research workbench
D116A mutant of SO1698 protein, an aspartic peptidase from shewanella oneidensis, at PH7.5
Analyse D116A mutant of SO1698 protein, an aspartic peptidase from shewanella… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3NJL
- Type
- protein
- Length
- 119 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidase
- UniProt
- Q8EGA7
- Ligands
- MG
- Pockets
- 1 · best druggability 0.31
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidase | protein | 119 | 0% helix, 54% strand | Q8EGA7 |
Ligands and binding sites
- MG · Magnesium ion · metal · 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 | 79 | 0.31 | 0.73 | 16 | empty |
Compared structures
- 3NJL · D116A mutant of SO1698 protein, an aspartic peptidase from Shewanella oneidensis, at pH7.5 · 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 Q8EGA7
- Elsewhere: RCSB PDB 3NJL · PDBe 3NJL · UniProt Q8EGA7
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