Research workbench
The crystal structure of human lambda-crystallin, CRYL1
Analyse The crystal structure of human lambda-crystallin, CRYL1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3F3S
- Type
- protein
- Length
- 623 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lambda-crystallin homolog
- UniProt
- Q9Y2S2
- Ligands
- NAD, SO4, CL
- Pockets
- 9 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 55% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lambda-crystallin homolog | protein | 312 | 55% helix, 11% strand | Q9Y2S2 |
| B | Lambda-crystallin homolog | protein | 311 | 55% helix, 12% strand | Q9Y2S2 |
Ligands and binding sites
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
- CL · Chloride ion · ion · 4 copies · chains A, B
- GOL · Glycerol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 576 | 0.77 | 0.83 | 60 | NAD, SO4, GOL |
| 2 | 426 | 0.67 | 0.80 | 45 | NAD, SO4 |
| 3 | 225 | 0.55 | 0.77 | 23 | empty |
| 4 | 139 | 0.53 | 0.81 | 20 | empty |
| 5 | 209 | 0.51 | 0.77 | 38 | empty |
Interfaces
1 interface between chains.
- A–B · 5344 Ų buried · 52 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 Q9Y2S2
- Elsewhere: RCSB PDB 3F3S · PDBe 3F3S · UniProt Q9Y2S2
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