Research workbench
Human annexin A2 with heparin tetrasaccharide bound
Analyse Human annexin A2 with heparin tetrasaccharide bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HYU
- Type
- protein
- Length
- 308 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Annexin A2
- UniProt
- P07355
- Ligands
- UAP, SGN, IDS, CA
- Pockets
- 5 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 73% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Annexin A2 | protein | 308 | 73% helix, 0% strand | P07355 |
Ligands and binding sites
- UAP · 4-deoxy-2-O-sulfo-alpha-L-threo-hex-4-enopyranuronic acid · ligand · chains A
- SGN · 2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose · sugar · 2 copies · chains A
- IDS · 2-O-sulfo-alpha-L-idopyranuronic acid · sugar · chains A
- CA · Calcium ion · metal · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 86 | 0.48 | 0.82 | 23 | empty |
| 2 | 77 | 0.46 | 0.82 | 21 | empty |
| 3 | 97 | 0.37 | 0.75 | 17 | empty |
| 4 | 66 | 0.32 | 0.76 | 15 | empty |
| 5 | 50 | 0.27 | 0.74 | 14 | 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 P07355
- Elsewhere: RCSB PDB 2HYU · PDBe 2HYU · UniProt P07355
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