Research workbench
RPN11 homolog from caldiarchaeum subterraneum, truncated
Analyse RPN11 homolog from caldiarchaeum subterraneum, truncated in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FJV
- Type
- protein
- Length
- 148 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 26S proteasome regulatory subunit N11-like protein
- UniProt
- E6N8B9
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 32% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 26S proteasome regulatory subunit N11-like protein | protein | 148 | 32% helix, 31% strand | E6N8B9 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6FJV · Rpn11 homolog from Caldiarchaeum Subterraneum, truncated · 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 E6N8B9
- Elsewhere: RCSB PDB 6FJV · PDBe 6FJV · UniProt E6N8B9
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