Research workbench
Beta appendage in complex with B-arrestin peptide
Analyse Beta appendage in complex with B-arrestin peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2IV8
- Type
- protein
- Length
- 250 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P63010, P49407
Structure
x-ray diffraction · 3 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 233 | — | P63010 |
| P | — | protein | 14 | — | P49407 |
| Q | — | protein | 3 | — | P49407 |
Compared structures
- 2IV8 · beta appendage in complex with b-arrestin peptide · the same entry in another collection · chain A against A, TM-score 1.00
- P63010 · AlphaFold monomer V2.0 prediction for ap-2 complex subunit beta (P63010) · a predicted model of the same protein · chain A against A, TM-score 0.98
- P49407 · AlphaFold monomer V2.0 prediction for beta-arrestin-1 (P49407) · a predicted model of the same protein · chain Q against A, TM-score 0.97
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 P63010
- Every structure of UniProt P49407
- Elsewhere: RCSB PDB 2IV8 · PDBe 2IV8 · UniProt P63010 · UniProt P49407
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