Research workbench
Pth-bound human PTH1R in complex with gs (CLASS2)
Analyse Pth-bound human PTH1R in complex with gs (CLASS2) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7VVL
- Type
- protein
- Length
- 1,126 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Guanine nucleotide-binding protein G(S) subunit alpha isoforms short; Guanine…
- UniProt
- P63092, P54311, P63212, P01270, Q03431
- Pockets
- 15 · best druggability 0.81
Structure
electron microscopy · 6 distinct chains · 37% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanine nucleotide-binding protein G(S) subunit alpha isoforms short | protein | 230 | 47% helix, 17% strand | P63092 |
| B | Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | protein | 335 | 6% helix, 47% strand | P54311 |
| G | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | protein | 53 | 51% helix, 0% strand | P63212 |
| N | Nanobody NB35 | protein | 128 | 5% helix, 42% strand | — |
| P | Parathyroid hormone | protein | 34 | 91% helix, 0% strand | P01270 |
| R | Parathyroid HORMONE/PARATHYROID hormone-related peptide receptor | protein | 346 | 66% helix, 4% strand | Q03431 |
Pockets
15 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 715 | 0.81 | 0.85 | 59 | empty |
| 2 | 372 | 0.71 | 0.83 | 50 | empty |
| 3 | 1104 | 0.70 | 0.75 | 63 | empty |
| 4 | 691 | 0.70 | 0.77 | 58 | empty |
| 5 | 157 | 0.65 | 0.86 | 25 | empty |
Interfaces
7 interfaces between chains.
- B–G · 2016 Ų buried · 15 hydrogen bonds · protein-protein
- P–R · 1897 Ų buried · 19 hydrogen bonds · protein-protein
- A–B · 1472 Ų buried · 25 hydrogen bonds · protein-protein
- A–R · 970 Ų buried · 6 hydrogen bonds · protein-protein
- A–N · 909 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 7VVL · PTH-bound human PTH1R in complex with Gs (class2) · the same entry in another collection · chain R against R, TM-score 1.00
- P54311 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(I)/G(S)/G(T)… · a predicted model of the same protein · chain B against A, TM-score 1.00
- Q03431 · AlphaFold monomer V2.0 prediction for parathyroid HORMONE/PARATHYROID hormone-related… · a predicted model of the same protein · chain R against A, TM-score 0.95
- P01270 · AlphaFold monomer V2.0 prediction for parathyroid hormone (P01270) · a predicted model of the same protein · chain P against A, TM-score 0.90
- P63212 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(I)/G(S)/G(O)… · a predicted model of the same protein · chain G against A, TM-score 0.66
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 P63092
- Every structure of UniProt P54311
- Every structure of UniProt P63212
- Every structure of UniProt P01270
- Every structure of UniProt Q03431
- Elsewhere: RCSB PDB 7VVL · PDBe 7VVL · UniProt P63092 · UniProt P54311 · UniProt P63212 · UniProt P01270 · UniProt Q03431
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