Research workbench
Cryoem structure of human PAC1 receptor in complex with maxadilan
Analyse Cryoem structure of human PAC1 receptor in complex with maxadilan in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6M1H
- Type
- protein
- Length
- 1,139 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pituitary adenylate cyclase-activating polypeptide type I receptor; Maxadilan; Nanobody…
- UniProt
- P30659, P59768, P62873
- Pockets
- 15 · best druggability 0.83
Structure
electron microscopy · 6 distinct chains · 33% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Pituitary adenylate cyclase-activating polypeptide type I receptor | protein | 341 | 56% helix, 6% strand | — |
| B | Maxadilan | protein | 61 | 64% helix, 0% strand | P30659 |
| C | Nanobody 35 | protein | 126 | 5% helix, 38% strand | — |
| D | Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 | protein | 57 | 51% helix, 0% strand | P59768 |
| E | Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 | protein | 338 | 8% helix, 42% strand | P62873 |
| F | Guanine nucleotide-binding protein G(S) subunit alpha isoforms short | protein | 216 | 38% helix, 16% strand | — |
Pockets
15 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 867 | 0.83 | 0.85 | 73 | empty |
| 2 | 864 | 0.75 | 0.79 | 64 | empty |
| 3 | 745 | 0.75 | 0.80 | 86 | empty |
| 4 | 967 | 0.74 | 0.77 | 71 | empty |
| 5 | 75 | 0.73 | 0.97 | 22 | empty |
Interfaces
7 interfaces between chains.
- D–E · 2221 Ų buried · 14 hydrogen bonds · protein-protein
- A–B · 2009 Ų buried · 12 hydrogen bonds · protein-protein
- E–F · 1379 Ų buried · 11 hydrogen bonds · protein-protein
- A–F · 1071 Ų buried · 6 hydrogen bonds · protein-protein
- C–F · 832 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 7 disulfide (disulfide).
Compared structures
- 6M1H · CryoEM structure of human PAC1 receptor in complex with maxadilan · the same entry in another collection · chain F against F, TM-score 1.00
- P62873 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(I)/G(S)/G(T)… · a predicted model of the same protein · chain E against A, TM-score 0.99
- P30659 · AlphaFold monomer V2.0 prediction for maxadilan (P30659) · a predicted model of the same protein · chain B against A, TM-score 0.88
- P59768 · AlphaFold monomer V2.0 prediction for guanine nucleotide-binding protein G(I)/G(S)/G(O)… · a predicted model of the same protein · chain D against A, TM-score 0.85
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 P30659
- Every structure of UniProt P59768
- Every structure of UniProt P62873
- Elsewhere: RCSB PDB 6M1H · PDBe 6M1H · UniProt P30659 · UniProt P59768 · UniProt P62873
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