Research workbench
Pth-bound human PTH1R in complex with gs (CLASS3)
Analyse Pth-bound human PTH1R in complex with gs (CLASS3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7VVM
- Type
- protein
- Length
- 1,133 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
- 14 · best druggability 0.81
Structure
electron microscopy · 6 distinct chains · 37% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Guanine nucleotide-binding protein G(S) subunit alpha isoforms short | protein | 230 | 46% helix, 15% strand | P63092 |
| B | Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | protein | 335 | 7% helix, 45% strand | P54311 |
| G | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | protein | 54 | 57% helix, 0% strand | P63212 |
| N | Nanobody NB35 | protein | 128 | 5% helix, 39% strand | — |
| P | Parathyroid hormone | protein | 32 | 91% helix, 0% strand | P01270 |
| R | Parathyroid HORMONE/PARATHYROID hormone-related peptide receptor | protein | 354 | 64% helix, 5% strand | Q03431 |
Pockets
14 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 682 | 0.81 | 0.85 | 55 | empty |
| 2 | 173 | 0.70 | 0.89 | 23 | empty |
| 3 | 316 | 0.70 | 0.84 | 45 | empty |
| 4 | 634 | 0.69 | 0.78 | 60 | empty |
| 5 | 656 | 0.69 | 0.77 | 60 | empty |
Interfaces
7 interfaces between chains.
- B–G · 2019 Ų buried · 15 hydrogen bonds · protein-protein
- A–B · 1510 Ų buried · 24 hydrogen bonds · protein-protein
- P–R · 1238 Ų buried · 9 hydrogen bonds · protein-protein
- A–R · 1012 Ų buried · 4 hydrogen bonds · protein-protein
- A–N · 901 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 7VVM · PTH-bound human PTH1R in complex with Gs (class3) · 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 0.81
- 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 0.65
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 7VVM · PDBe 7VVM · UniProt P63092 · UniProt P54311 · UniProt P63212 · UniProt P01270 · UniProt Q03431
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