Research workbench
Crystal structure of a mutant of rat annexin A5
Analyse Crystal structure of a mutant of rat annexin A5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2H0K
- Type
- protein
- Length
- 636 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Annexin A5
- UniProt
- P14668
- Ligands
- CA
- Pockets
- 10 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 71% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Annexin A5 | protein | 318 | 71% helix, 0% strand | P14668 |
Ligands and binding sites
- CA · Calcium ion · metal · 22 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 112 | 0.56 | 0.84 | 24 | empty |
| 2 | 126 | 0.53 | 0.82 | 20 | empty |
| 3 | 109 | 0.52 | 0.82 | 27 | empty |
| 4 | 124 | 0.51 | 0.81 | 23 | empty |
| 5 | 121 | 0.46 | 0.78 | 24 | empty |
Interfaces
1 interface between chains.
- A–B · 560 Ų buried · 8 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 P14668
- Elsewhere: RCSB PDB 2H0K · PDBe 2H0K · UniProt P14668
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