Research workbench
Human SMP30/GNL-1,5-ag complex
Analyse Human 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
- 4GNC
- Type
- protein
- Length
- 595 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Regucalcin
- EC
- 3.1.1.17
- UniProt
- Q15493
- Ligands
- ASO, CA
- Pockets
- 3 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Regucalcin (EC 3.1.1.17) | protein | 298 | 5% helix, 55% strand | Q15493 |
| B | Regucalcin (EC 3.1.1.17) | protein | 297 | 6% helix, 56% strand | Q15493 |
Ligands and binding sites
- ASO · 1,5-anhydro-D-glucitol · ligand · 5 copies · chains A, B
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 126 | 0.80 | 0.98 | 34 | empty |
| 2 | 123 | 0.79 | 0.97 | 32 | empty |
| 3 | 1051 | 0.77 | 0.79 | 98 | ASO |
Interfaces
1 interface between chains.
- A–B · 325 Ų buried · 7 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 Q15493
- Elsewhere: RCSB PDB 4GNC · PDBe 4GNC · UniProt Q15493
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