Research workbench
Xenopus RSPO2 FU1-FU2 crystal form I
Analyse Xenopus RSPO2 FU1-FU2 crystal form I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4C8V
- Type
- protein
- Length
- 871 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- R-spondin-2
- UniProt
- Q5M7L6
- Pockets
- 10 · best druggability 0.58
Structure
x-ray diffraction · 6 distinct chains · 0% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | R-spondin-2 | protein | 115 | 0% helix, 50% strand | Q5M7L6 |
| B | R-spondin-2 | protein | 112 | 0% helix, 46% strand | Q5M7L6 |
| C | R-spondin-2 | protein | 113 | 0% helix, 48% strand | Q5M7L6 |
| D | R-spondin-2 | protein | 110 | 0% helix, 49% strand | Q5M7L6 |
| E, F, G | R-spondin-2 | protein | 105 | 0% helix, 49% strand | Q5M7L6 |
| H | R-spondin-2 | protein | 106 | 0% helix, 53% strand | Q5M7L6 |
Pockets
10 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 332 | 0.58 | 0.77 | 39 | empty |
| 2 | 207 | 0.49 | 0.76 | 36 | empty |
| 3 | 186 | 0.47 | 0.75 | 26 | empty |
| 4 | 154 | 0.46 | 0.76 | 27 | empty |
| 5 | 102 | 0.36 | 0.74 | 23 | empty |
Interfaces
8 interfaces between chains.
- F–H · 605 Ų buried · 9 hydrogen bonds · protein-protein
- A–F · 542 Ų buried · 8 hydrogen bonds · protein-protein
- D–F · 490 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 470 Ų buried · 5 hydrogen bonds · protein-protein
- A–C · 446 Ų buried · 7 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 64 disulfide (disulfide).
Compared structures
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 Q5M7L6
- Elsewhere: RCSB PDB 4C8V · PDBe 4C8V · UniProt Q5M7L6
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