Research workbench
Crystal structure of human senescence marker protein-30(SMP30)(CALCIUM bound)
Analyse Crystal structure of human senescence marker protein-30(SMP30)(CALCIUM bound) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3G4E
- Type
- protein
- Length
- 594 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Regucalcin
- UniProt
- Q15493
- Ligands
- CA
- Pockets
- 6 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Regucalcin | protein | 297 | 5% helix, 55% strand | Q15493 |
Ligands and binding sites
- 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
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.78 | 0.98 | 26 | empty |
| 2 | 93 | 0.77 | 0.98 | 27 | empty |
| 3 | 176 | 0.64 | 0.85 | 26 | empty |
| 4 | 142 | 0.64 | 0.86 | 26 | empty |
| 5 | 378 | 0.59 | 0.76 | 37 | empty |
Interfaces
1 interface between chains.
- A–B · 419 Ų buried · 5 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 3G4E · PDBe 3G4E · UniProt Q15493
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