MolNFT v1 · #101215 · protein
Crystal structure of SSPH1 lrr domain
4NKH · E3 ubiquitin-protein ligase SSPH1: “Crystal structure of SSPH1 lrr domain”. X-ray diffraction, 15 pockets (best druggability 0.78). MolNFT v1 #101215 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4NKH
- Type
- protein
- Length
- 1,416 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase SSPH1
- EC
- 6.3.2.-
- UniProt
- D0ZVG2
- Pockets
- 15 · best druggability 0.78
Structure
x-ray diffraction · 6 distinct chains · 19% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase SSPH1 (EC 6.3.2.-) | protein | 236 | 19% helix, 14% strand | D0ZVG2 |
| B | E3 ubiquitin-protein ligase SSPH1 (EC 6.3.2.-) | protein | 237 | 18% helix, 14% strand | D0ZVG2 |
| C | E3 ubiquitin-protein ligase SSPH1 (EC 6.3.2.-) | protein | 233 | 18% helix, 14% strand | D0ZVG2 |
| D | E3 ubiquitin-protein ligase SSPH1 (EC 6.3.2.-) | protein | 236 | 19% helix, 14% strand | D0ZVG2 |
| E | E3 ubiquitin-protein ligase SSPH1 (EC 6.3.2.-) | protein | 239 | 20% helix, 14% strand | D0ZVG2 |
| F | E3 ubiquitin-protein ligase SSPH1 (EC 6.3.2.-) | protein | 235 | 18% helix, 14% strand | D0ZVG2 |
Pockets
15 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 121 | 0.78 | 0.96 | 35 | empty |
| 2 | 587 | 0.63 | 0.75 | 63 | empty |
| 3 | 409 | 0.56 | 0.74 | 47 | empty |
| 4 | 240 | 0.52 | 0.76 | 35 | empty |
| 5 | 218 | 0.51 | 0.76 | 30 | empty |
Interfaces
9 interfaces between chains.
- B–E · 1060 Ų buried · 7 hydrogen bonds · protein-protein
- A–F · 1038 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 1002 Ų buried · 9 hydrogen bonds · protein-protein
- A–B · 607 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 559 Ų buried · 10 hydrogen bonds · protein-protein
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 D0ZVG2
- Elsewhere: RCSB PDB 4NKH · PDBe 4NKH · UniProt D0ZVG2
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