Research workbench
Crystal structure of human CRFR2 alpha extracellular domain in complex with urocortin 2
Analyse Crystal structure of human CRFR2 alpha extracellular domain in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3N95
- Type
- protein
- Length
- 1,899 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltose binding protein-CRFR2 alpha extracellular domain; Urocortin-2
- UniProt
- Q96RP3
- Ligands
- GLC, NH2
- Pockets
- 19 · best druggability 0.78
Structure
x-ray diffraction · 5 distinct chains · 42% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maltose binding protein-CRFR2 alpha extracellular domain | protein | 470 | 41% helix, 22% strand | — |
| B | Maltose binding protein-CRFR2 alpha extracellular domain | protein | 472 | 41% helix, 21% strand | — |
| C | Maltose binding protein-CRFR2 alpha extracellular domain | protein | 462 | 41% helix, 22% strand | — |
| D | Maltose binding protein-CRFR2 alpha extracellular domain | protein | 463 | 41% helix, 22% strand | — |
| E, F | Urocortin-2 | protein | 16 | 88% helix, 0% strand | Q96RP3 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 8 copies · chains A, B, C, D
- NH2 · Amino group · ion · 2 copies · chains C, E, D, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 974 | 0.78 | 0.80 | 105 | empty |
| 2 | 275 | 0.73 | 0.86 | 30 | GLC |
| 3 | 851 | 0.73 | 0.78 | 58 | empty |
| 4 | 279 | 0.72 | 0.86 | 31 | GLC |
| 5 | 790 | 0.72 | 0.77 | 61 | empty |
Interfaces
6 interfaces between chains.
- B–D · 1617 Ų buried · 18 hydrogen bonds · protein-protein
- A–C · 1583 Ų buried · 14 hydrogen bonds · protein-protein
- C–E · 776 Ų buried · 6 hydrogen bonds · protein-protein
- D–F · 752 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 298 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 12 disulfide (disulfide).
Compared structures
- 3N95 · Crystal structure of human CRFR2 alpha extracellular domain in complex with Urocortin 2 · the same entry in another collection · chain B against B, TM-score 1.00
- Q96RP3 · AlphaFold monomer V2.0 prediction for urocortin-2 (Q96RP3) · a predicted model of the same protein · chain E 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 Q96RP3
- Elsewhere: RCSB PDB 3N95 · PDBe 3N95 · UniProt Q96RP3
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