Research workbench
Crystal structure of TYR24 phosphorylated annexin A2 at 3.4 a resolution
Analyse Crystal structure of TYR24 phosphorylated annexin A2 at 3.4 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5LQ2
- Type
- protein
- Length
- 638 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Annexin A2
- UniProt
- P07355
- Ligands
- CA
- Pockets
- 5 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Annexin A2 | protein | 319 | 68% helix, 0% strand | P07355 |
Ligands and binding sites
- CA · Calcium ion · metal · 10 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1015 | 0.74 | 0.77 | 95 | empty |
| 2 | 150 | 0.55 | 0.82 | 22 | empty |
| 3 | 145 | 0.51 | 0.80 | 23 | empty |
| 4 | 170 | 0.51 | 0.78 | 37 | empty |
| 5 | 58 | 0.27 | 0.73 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 208 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (phosphorylation).
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 P07355
- Elsewhere: RCSB PDB 5LQ2 · PDBe 5LQ2 · UniProt P07355
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