Research workbench
The closed conformation of the sigma-1 receptor from xenopus laevis
Analyse The closed conformation of the sigma-1 receptor from xenopus laevis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7W2B
- Type
- protein
- Length
- 2,590 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q6DCU6
- Ligands
- AU
Structure
x-ray diffraction · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, F, H, L | — | protein | 215 | — | Q6DCU6 |
| D | — | protein | 221 | — | Q6DCU6 |
| B, G | — | protein | 219 | — | Q6DCU6 |
| I | — | protein | 217 | — | Q6DCU6 |
| J | — | protein | 210 | — | Q6DCU6 |
| K | — | protein | 214 | — | Q6DCU6 |
Ligands and binding sites
- AU · Gold ion · metal · 24 copies · chains A, C, E, D, L, F, B, G, H, I, J, K
- BOG · octyl beta-D-glucopyranoside · additive · 9 copies · chains A, E, C, D, B, F, G, I, K, H, J, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7W2B · The closed conformation of the sigma-1 receptor from Xenopus laevis · the same entry in another collection · chain L against L, 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 Q6DCU6
- Elsewhere: RCSB PDB 7W2B · PDBe 7W2B · UniProt Q6DCU6
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