Research workbench
Crystal structure of ca-bound human annexin A5 in low salt condition
Analyse Crystal structure of ca-bound human annexin A5 in low salt condition in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6K22
- Type
- protein
- Length
- 316 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Annexin A5
- UniProt
- P08758
- Ligands
- CA
- Pockets
- 4 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 69% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Annexin A5 | protein | 316 | 69% helix, 0% strand | P08758 |
Ligands and binding sites
- CA · Calcium ion · metal · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 153 | 0.52 | 0.79 | 35 | empty |
| 2 | 102 | 0.45 | 0.79 | 19 | empty |
| 3 | 83 | 0.44 | 0.81 | 23 | empty |
| 4 | 96 | 0.42 | 0.78 | 13 | empty |
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 P08758
- Elsewhere: RCSB PDB 6K22 · PDBe 6K22 · UniProt P08758
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