Research workbench
Crystal structure of the human LIN28B cold shock domain
Analyse Crystal structure of the human LIN28B cold shock domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4A4I
- Type
- protein
- Length
- 169 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein lin-28 homolog B
- UniProt
- Q6ZN17
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.39
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein lin-28 homolog B | protein | 84 | 7% helix, 55% strand | Q6ZN17 |
| B | Protein lin-28 homolog B | protein | 85 | 7% helix, 59% strand | Q6ZN17 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 112 | 0.39 | 0.75 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 354 Ų buried · 4 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 Q6ZN17
- Elsewhere: RCSB PDB 4A4I · PDBe 4A4I · UniProt Q6ZN17
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