Research workbench
Structure of ZNRF3-RSPO1
Analyse Structure of ZNRF3-RSPO1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4CDK
- Type
- protein
- Length
- 1,040 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase ZNRF3; R-spondin-1
- UniProt
- Q5SSZ7, Q2MKA7
- Pockets
- 17 · best druggability 0.76
Structure
x-ray diffraction · 8 distinct chains · 14% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase ZNRF3 | protein | 152 | 24% helix, 36% strand | Q5SSZ7 |
| B | E3 ubiquitin-protein ligase ZNRF3 | protein | 156 | 22% helix, 35% strand | Q5SSZ7 |
| C | E3 ubiquitin-protein ligase ZNRF3 | protein | 155 | 22% helix, 35% strand | Q5SSZ7 |
| D | E3 ubiquitin-protein ligase ZNRF3 | protein | 152 | 24% helix, 36% strand | Q5SSZ7 |
| E | R-spondin-1 | protein | 110 | 0% helix, 42% strand | Q2MKA7 |
| F | R-spondin-1 | protein | 103 | 0% helix, 41% strand | Q2MKA7 |
| G | R-spondin-1 | protein | 107 | 0% helix, 40% strand | Q2MKA7 |
| H | R-spondin-1 | protein | 105 | 0% helix, 36% strand | Q2MKA7 |
Pockets
17 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1165 | 0.76 | 0.78 | 97 | empty |
| 2 | 74 | 0.68 | 0.94 | 16 | empty |
| 3 | 362 | 0.62 | 0.78 | 45 | empty |
| 4 | 262 | 0.62 | 0.80 | 38 | empty |
| 5 | 172 | 0.60 | 0.82 | 35 | empty |
Interfaces
12 interfaces between chains.
- A–B · 1268 Ų buried · 29 hydrogen bonds · protein-protein
- C–D · 1258 Ų buried · 31 hydrogen bonds · protein-protein
- C–G · 1248 Ų buried · 17 hydrogen bonds · protein-protein
- A–E · 1186 Ų buried · 17 hydrogen bonds · protein-protein
- B–F · 1008 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 34 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 Q5SSZ7
- Every structure of UniProt Q2MKA7
- Elsewhere: RCSB PDB 4CDK · PDBe 4CDK · UniProt Q5SSZ7 · UniProt Q2MKA7
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