Research workbench
Monellin (mnei) at 1.15 resolution
Analyse Monellin (mnei) at 1.15 resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2O9U
- Type
- protein
- Length
- 96 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Monellin chain B and monellin chain a
- UniProt
- P02882, P02881
- Ligands
- SO4
Structure
x-ray diffraction · 1 distinct chain · 18% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Monellin chain B and monellin chain a | protein | 96 | 18% helix, 48% strand | P02882, P02881 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains X
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2O9U · Monellin (MNEI) at 1.15 resolution · the same entry in another collection · chain X against X, TM-score 1.00
- P02882 · AlphaFold monomer V2.0 prediction for monellin chain B (P02882) · a predicted model of the same protein · chain X against A, TM-score 0.50
- P02881 · AlphaFold monomer V2.0 prediction for monellin chain a (P02881) · a predicted model of the same protein · chain X against A, TM-score 0.43
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 P02882
- Every structure of UniProt P02881
- Elsewhere: RCSB PDB 2O9U · PDBe 2O9U · UniProt P02882 · UniProt P02881
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