Research workbench
Mouse SMP30/GNL-1,5-ag complex
Analyse Mouse SMP30/GNL-1,5-ag complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GN8
- Type
- protein
- Length
- 594 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Regucalcin
- EC
- 3.1.1.17
- UniProt
- Q64374
- Ligands
- ASO, CA, SO4
- Pockets
- 7 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 57% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Regucalcin (EC 3.1.1.17) | protein | 297 | 6% helix, 57% strand | Q64374 |
Ligands and binding sites
- ASO · 1,5-anhydro-D-glucitol · ligand · 9 copies · chains A, B
- CA · Calcium ion · metal · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 13 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 110 | 0.78 | 0.97 | 29 | empty |
| 2 | 120 | 0.78 | 0.96 | 31 | empty |
| 3 | 76 | 0.73 | 0.97 | 19 | empty |
| 4 | 475 | 0.73 | 0.82 | 56 | ASO, SO4 |
| 5 | 125 | 0.51 | 0.81 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 872 Ų buried · 15 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 Q64374
- Elsewhere: RCSB PDB 4GN8 · PDBe 4GN8 · UniProt Q64374
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