MolNFT v1 · #9131 · protein
X-ray structure of full-length annexin 1
1HM6: “X-ray structure of full-length annexin 1”. X-ray diffraction, 1 ligand (SO4), 8 pockets (best druggability 0.84). MolNFT v1 #9131 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1HM6
- Type
- protein
- Length
- 686 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Annexin 1
- UniProt
- P19619
- Ligands
- SO4
- Pockets
- 8 · best druggability 0.84
Structure
x-ray diffraction · 1 distinct chain · 70% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Annexin 1 | protein | 343 | 70% helix, 1% strand | P19619 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 12 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1167 | 0.84 | 0.85 | 104 | empty |
| 2 | 231 | 0.53 | 0.77 | 40 | empty |
| 3 | 110 | 0.52 | 0.82 | 21 | empty |
| 4 | 89 | 0.51 | 0.84 | 22 | empty |
| 5 | 210 | 0.51 | 0.76 | 40 | empty |
Interfaces
1 interface between chains.
- A–B · 1543 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
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 P19619
- Elsewhere: RCSB PDB 1HM6 · PDBe 1HM6 · UniProt P19619
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