Research workbench
Crystal structure of human CRFR2 alpha extracellular domain in complex with urocortin 3
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
- 3N93
- Type
- protein
- Length
- 951 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Maltose binding protein-CRFR2 alpha; Urocortin-3
- UniProt
- Q969E3
- Ligands
- GLC, NH2
- Pockets
- 8 · best druggability 0.78
Structure
x-ray diffraction · 3 distinct chains · 42% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Maltose binding protein-CRFR2 alpha | protein | 471 | 42% helix, 22% strand | — |
| B | Maltose binding protein-CRFR2 alpha | protein | 464 | 42% helix, 23% strand | — |
| C | Urocortin-3 | protein | 16 | 88% helix, 0% strand | Q969E3 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 4 copies · chains A, B
- NH2 · Amino group · ion · chains B, C
- GOL · Glycerol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1148 | 0.78 | 0.80 | 99 | GLC, GOL |
| 2 | 317 | 0.70 | 0.84 | 36 | GLC |
| 3 | 539 | 0.69 | 0.79 | 48 | empty |
| 4 | 542 | 0.68 | 0.78 | 60 | empty |
| 5 | 176 | 0.46 | 0.75 | 25 | empty |
Interfaces
2 interfaces between chains.
- A–B · 1655 Ų buried · 12 hydrogen bonds · protein-protein
- B–C · 745 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 3N93 · Crystal structure of human CRFR2 alpha extracellular domain in complex with Urocortin 3 · the same entry in another collection · chain B against B, TM-score 1.00
- Q969E3 · AlphaFold monomer V2.0 prediction for urocortin-3 (Q969E3) · a predicted model of the same protein · chain C against A, TM-score 0.82
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 Q969E3
- Elsewhere: RCSB PDB 3N93 · PDBe 3N93 · UniProt Q969E3
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