Research workbench
Human endothelin receptor type-B in complex with et-1
Analyse Human endothelin receptor type-B in complex with et-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5GLH
- Type
- protein
- Length
- 473 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endothelin receptor subtype-B; Peptide from endothelin-1
- UniProt
- P05305
- Pockets
- 5 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 72% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endothelin receptor subtype-B | protein | 452 | 73% helix, 6% strand | — |
| B | Peptide from endothelin-1 | protein | 21 | 43% helix, 0% strand | P05305 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 230 | 0.59 | 0.79 | 32 | empty |
| 2 | 63 | 0.52 | 0.86 | 19 | empty |
| 3 | 106 | 0.51 | 0.82 | 20 | empty |
| 4 | 115 | 0.41 | 0.76 | 19 | empty |
| 5 | 161 | 0.40 | 0.73 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 1602 Ų buried · 22 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
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 P05305
- Elsewhere: RCSB PDB 5GLH · PDBe 5GLH · UniProt P05305
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