Research workbench
D116A mutant of SO1698 protein, an aspartic peptidase from shewanella oneidensis, at PH5.5
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
- 3NJK
- Type
- protein
- Length
- 122 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidase
- UniProt
- Q8EGA7
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidase | protein | 122 | 0% helix, 54% strand | Q8EGA7 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3NJK · D116A mutant of SO1698 protein, an aspartic peptidase from Shewanella oneidensis, at pH5.5 · 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 3NJK · PDBe 3NJK · UniProt Q8EGA7
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