MolNFT v1 · #106102 · protein
Crystal structure of the L27 domain of discs large 1 (target id nysgrc-010766) from drosophila melanogaster (space group P21)
4RP5 · Disks large 1 tumor suppressor protein: “Crystal structure of the L27 domain of discs large 1 (target id nysgrc-010766) from drosophila melanogaster…”. X-ray diffraction, 1 ligand (CL), 1 pocket (best druggability 0.55). MolNFT v1…
- PDB
- 4RP5
- Type
- protein
- Length
- 184 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Disks large 1 tumor suppressor protein
- UniProt
- P31007
- Ligands
- CL
- Pockets
- 1 · best druggability 0.55
Structure
x-ray diffraction · 2 distinct chains · 74% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Disks large 1 tumor suppressor protein | protein | 94 | 72% helix, 4% strand | P31007 |
| B | Disks large 1 tumor suppressor protein | protein | 90 | 76% helix, 6% strand | P31007 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 290 | 0.55 | 0.76 | 34 | empty |
Interfaces
1 interface between chains.
- A–B · 2572 Ų buried · 21 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (engineered).
Compared structures
- 4RP5 · Crystal Structure of the L27 domain of Discs Large 1 (target ID NYSGRC-010766) from… · the same entry in another collection · chain B against B, TM-score 1.00
- P31007 · AlphaFold monomer V2.0 prediction for disks large 1 tumor suppressor protein (P31007) · a predicted model of the same protein · chain B against A, TM-score 0.49
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 P31007
- Elsewhere: RCSB PDB 4RP5 · PDBe 4RP5 · UniProt P31007
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