Research workbench
Crystal structure of the a variant of human ALPHA1-acid glycoprotein and disopyramide complex
Analyse Crystal structure of the a variant of human ALPHA1-acid glycoprotein and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3APW
- Type
- protein
- Length
- 351 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P19652
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 175 | — | P19652 |
| B | — | protein | 176 | — | P19652 |
Compared structures
- 3APW · Crystal structure of the A variant of human alpha1-acid glycoprotein and disopyramide… · 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 3APW · PDBe 3APW · UniProt P19652
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