Research workbench
Crystal structure of the extracellular domain of human RAMP2
Analyse Crystal structure of the extracellular domain of human RAMP2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3AQE
- Type
- protein
- Length
- 450 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Receptor activity-modifying protein 2
- UniProt
- O60895
- Pockets
- 7 · best druggability 0.80
Structure
x-ray diffraction · 4 distinct chains · 78% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, E | Receptor activity-modifying protein 2 | protein | 76 | 76% helix, 0% strand | O60895 |
| C | Receptor activity-modifying protein 2 | protein | 73 | 79% helix, 0% strand | O60895 |
| D | Receptor activity-modifying protein 2 | protein | 74 | 78% helix, 0% strand | O60895 |
| F | Receptor activity-modifying protein 2 | protein | 75 | 77% helix, 0% strand | O60895 |
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 584 | 0.80 | 0.85 | 64 | empty |
| 2 | 198 | 0.68 | 0.86 | 22 | empty |
| 3 | 181 | 0.48 | 0.76 | 28 | empty |
| 4 | 153 | 0.41 | 0.73 | 18 | empty |
| 5 | 157 | 0.41 | 0.73 | 19 | empty |
Interfaces
9 interfaces between chains.
- E–F · 714 Ų buried · 10 hydrogen bonds · protein-protein
- D–F · 709 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 701 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 679 Ų buried · 6 hydrogen bonds · protein-protein
- D–E · 624 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide, 12 modified (disulfide, engineered).
Compared structures
- 3AQE · Crystal structure of the extracellular domain of human RAMP2 · the same entry in another collection · chain F against F, TM-score 1.00
- O60895 · AlphaFold monomer V2.0 prediction for receptor activity-modifying protein 2 (O60895) · a predicted model of the same protein · chain C against A, TM-score 0.96
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 O60895
- Elsewhere: RCSB PDB 3AQE · PDBe 3AQE · UniProt O60895
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