Research workbench
ROR(GAMMA)T ligand binding domain in complex with 20-alpha- hydroxycholesterol and allosteric ligand FM26
Analyse ROR(GAMMA)T ligand binding domain in complex with 20-alpha- hydroxycholesterol… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6T4T
- Type
- protein
- Length
- 241 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P51449
- Ligands
- L3E, HCD
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 241 | — | P51449 |
Ligands and binding sites
- L3E · 4-[(~{E})-[3-[2-chloranyl-6-(trifluoromethyl)phenyl]-5-(1~{H}-pyrrol-3-yl)-1,2-oxazol-4-yl]methylideneamino]benzoic acid · ligand · chains A
- HCD · (3alpha,8alpha)-cholest-5-ene-3,20-diol · ligand · chains A
- GOL · Glycerol · additive · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6T4T · ROR(gamma)t ligand binding domain in complex with 20-alpha-hydroxycholesterol and… · 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
- Every structure of UniProt P51449
- Elsewhere: RCSB PDB 6T4T · PDBe 6T4T · UniProt P51449
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