Research workbench
The structure of CA2+-loaded S100A2 at 1.3A resolution
Analyse The structure of CA2+-loaded S100A2 at 1.3A resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4DUQ
- Type
- protein
- Length
- 178 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein S100-A2
- UniProt
- P29034
- Ligands
- CA
- Pockets
- 1 · best druggability 0.32
Structure
x-ray diffraction · 2 distinct chains · 69% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein S100-A2 | protein | 88 | 68% helix, 2% strand | P29034 |
| B | Protein S100-A2 | protein | 90 | 69% helix, 2% strand | P29034 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains A, B
- 15P · Polyethylene glycol (N=34) · additive · 2 copies · chains B, A
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 | 66 | 0.32 | 0.74 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 1325 Ų buried · 13 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 P29034
- Elsewhere: RCSB PDB 4DUQ · PDBe 4DUQ · UniProt P29034
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