MolNFT v1 · #43176 · protein
NMR structure of the GCN4 trigger peptide refined using biased molecular dynamics simulations
2L56 · General control protein GCN4: “NMR structure of the GCN4 trigger peptide refined using biased molecular dynamics simulations”. Solution nmr, 2 ligands (ACE, NH2). MolNFT v1 #43176 on GenesisL1: 3D structure, binding sites and…
- PDB
- 2L56
- Type
- protein
- Length
- 16 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- General control protein GCN4
- Ligands
- ACE, NH2
Structure
solution nmr · 1 distinct chain · 63% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | General control protein GCN4 | protein | 16 | 63% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 2L56 · NMR structure of the GCN4 trigger peptide refined using biased molecular dynamics… · 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
- Elsewhere: RCSB PDB 2L56 · PDBe 2L56
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