MolNFT v1 · #72323 · protein
SO1698 protein, an aspartic peptidase from shewanella oneidensis.
3N55: “SO1698 protein, an aspartic peptidase from shewanella oneidensis.”. X-ray diffraction, 1 ligand (ZN). MolNFT v1 #72323 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3N55
- Type
- protein
- Length
- 118 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Peptidase
- UniProt
- Q8EGA7
- Ligands
- ZN
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Peptidase | protein | 111 | 0% helix, 55% strand | Q8EGA7 |
| B | Peptidase | protein | 7 | 0% helix, 57% strand | Q8EGA7 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
- BME · Beta-mercaptoethanol · additive · chains A
- ACT · Acetate ion · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 650 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent, 1 isopeptide, 1 modified (additive adduct, isopeptide, engineered).
Compared structures
- 3N55 · SO1698 protein, an aspartic peptidase from Shewanella oneidensis. · 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 3N55 · PDBe 3N55 · UniProt Q8EGA7
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