Research workbench
Structural basis of translational stalling by human cytomegalovirus (hcmv) and fungal arginine attenuator peptide (aap)
Analyse Structural basis of translational stalling by human cytomegalovirus (hcmv) and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XL1
- Type
- protein
- Length
- 15 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Arginine attenuator peptide
- UniProt
- P22702
Structure
solution nmr · 1 distinct chain · 87% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginine attenuator peptide | protein | 15 | 87% helix, 0% strand | P22702 |
Compared structures
- 2XL1 · Structural basis of translational stalling by human cytomegalovirus (hCMV) and fungal… · the same entry in another collection · chain A against A, TM-score 1.00
- P22702 · AlphaFold monomer V2.0 prediction for arginine attenuator peptide (P22702) · a predicted model of the same protein · chain A against A, TM-score 0.59
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 P22702
- Elsewhere: RCSB PDB 2XL1 · PDBe 2XL1 · UniProt P22702
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