MolNFT v1 · #145958 · protein
TRP-cage TR16B R16NVA : elimination of pH dependent interactions
6D37 · Ala-tyr-ala-gln-TRP-leu-ala-asp-dal-gly-pro-ala-ser-dal…: “TRP-cage TR16B R16NVA : elimination of pH dependent interactions”. Solution nmr, 2 ligands (ACE, NH2). MolNFT v1 #145958 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6D37
- Type
- protein
- Length
- 19 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ala-tyr-ala-gln-TRP-leu-ala-asp-dal-gly-pro-ala-ser-dal- nva-pro-pro-pro-ser
- Ligands
- ACE, NH2
Structure
solution nmr · 1 distinct chain · 47% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ala-tyr-ala-gln-TRP-leu-ala-asp-dal-gly-pro-ala-ser-dal- nva-pro-pro-pro-ser | protein | 19 | 47% 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: 2 d-amino, 1 covalent, 1 modified (D-amino acid, covalent ligand, nonstandard).
Compared structures
- 6D37 · Trp-cage tr16b R16Nva : Elimination of pH Dependent Interactions · 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 6D37 · PDBe 6D37
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