Research workbench
Crystal structure of the a variant of human ALPHA1-acid glycoprotein
Analyse Crystal structure of the a variant of human ALPHA1-acid glycoprotein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3APU
- Type
- protein
- Length
- 347 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Alpha-1-acid glycoprotein 2
- UniProt
- P19652
- Pockets
- 1 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Alpha-1-acid glycoprotein 2 | protein | 175 | 26% helix, 41% strand | P19652 |
| B | Alpha-1-acid glycoprotein 2 | protein | 172 | 25% helix, 41% strand | P19652 |
Ligands and binding sites
- PG4 · Tetraethylene glycol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1190 | 0.85 | 0.85 | 104 | PG4 |
Interfaces
1 interface between chains.
- A–B · 636 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 3APU · Crystal structure of the A variant of human alpha1-acid glycoprotein · the same entry in another collection · chain A against A, TM-score 1.00
- P19652 · AlphaFold monomer V2.0 prediction for alpha-1-acid glycoprotein 2 (P19652) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P19652
- Elsewhere: RCSB PDB 3APU · PDBe 3APU · UniProt P19652
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