Research workbench
Structure of the C-terminal domain of rage and its inhibitor
Analyse Structure of the C-terminal domain of rage and its inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VXG
- Type
- protein
- Length
- 16 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Advanced glycosylation end product-specific receptor
- UniProt
- Q15109
- Ligands
- RQV
Structure
solution nmr · 1 distinct chain · 0% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Advanced glycosylation end product-specific receptor | protein | 16 | 0% helix, 13% strand | Q15109 |
Ligands and binding sites
- RQV · N-(4-{7-cyano-4-[(morpholin-4-yl)methyl]quinolin-2-yl}phenyl)acetamide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6VXG · Structure of the C-terminal Domain of RAGE and Its Inhibitor · the same entry in another collection · chain A against A, TM-score 1.00
- Q15109 · AlphaFold monomer V2.0 prediction for advanced glycosylation end product-specific… · a predicted model of the same protein · chain A against A, TM-score 0.16
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 Q15109
- Elsewhere: RCSB PDB 6VXG · PDBe 6VXG · UniProt Q15109
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