Research workbench
Structure of /K. lactis/ DCP1-DCP2 decapping complex.
Analyse Structure of /K. lactis/ DCP1-DCP2 decapping complex. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LON
- Type
- protein
- Length
- 395 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- KLLA0F23980P; KLLA0E01827P
- UniProt
- Q6CIU1, Q6CPV9
- Pockets
- 7 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | KLLA0F23980P | protein | 221 | 42% helix, 13% strand | Q6CIU1 |
| B | KLLA0E01827P | protein | 174 | 23% helix, 36% strand | Q6CPV9 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 386 | 0.65 | 0.79 | 55 | empty |
| 2 | 162 | 0.48 | 0.77 | 18 | empty |
| 3 | 113 | 0.46 | 0.79 | 19 | empty |
| 4 | 110 | 0.40 | 0.75 | 19 | empty |
| 5 | 85 | 0.38 | 0.76 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 1710 Ų buried · 23 hydrogen bonds · protein-protein
Compared structures
- 5LON · Structure of /K. lactis/ Dcp1-Dcp2 decapping complex. · the same entry in another collection · chain A against A, TM-score 1.00
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 Q6CIU1
- Every structure of UniProt Q6CPV9
- Elsewhere: RCSB PDB 5LON · PDBe 5LON · UniProt Q6CIU1 · UniProt Q6CPV9
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