Research workbench
Crystal structure of rar-related orphan receptor C (nhis-RORGT(244- 487)-L6-SRC1(678-692)) in complex with an inverse agonist
Analyse Crystal structure of rar-related orphan receptor C (nhis-RORGT(244… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6VQF
- Type
- protein
- Length
- 252 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2
- Source
- Homo sapiens
- Molecule
- Nuclear receptor ROR-gamma
- UniProt
- P51449
- Ligands
- R7V
- Pockets
- 4 · best druggability 0.85
Structure
x-ray diffraction · resolution 2 · 1 distinct chain · 72% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nuclear receptor ROR-gamma | protein | 252 | 72% helix, 4% strand | P51449 |
Ligands and binding sites
- R7V · (1R,3S,4R)-4-[(3ar,9br)-9B-[(4-fluorophenyl)sulfonyl]-7-(1,1,1,2,3,3,3-heptafluoropropan-2-yl)-1,2,3A,4,5, 9B-hexahydro-3H-benzo[e]indole-3-carbonyl]-3-methylcyclohexane-1-carboxylic acid · ligand · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 470 | 0.85 | 0.91 | 39 | R7V, GOL |
| 2 | 128 | 0.46 | 0.77 | 17 | empty |
| 3 | 95 | 0.41 | 0.77 | 19 | empty |
| 4 | 62 | 0.30 | 0.75 | 16 | empty |
Compared structures
- 6VQF · Crystal structure of rar-related orphan receptor C (nhis-RORGT(244… · 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 6VQF · PDBe 6VQF · UniProt P51449
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