MolNFT v1 · #64765 · protein
Structure of an ARRESTIN/CLATHRIN complex reveals a novel clathrin binding domain that modulates receptor trafficking
3GD1: “Structure of an ARRESTIN/CLATHRIN complex reveals a novel clathrin binding domain that modulates receptor…”. X-ray diffraction. MolNFT v1 #64765 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3GD1
- Type
- protein
- Length
- 1,011 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P17870, P49951
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | — | protein | 345 | — | P17870 |
| E | — | protein | 300 | — | P17870 |
| I | — | protein | 358 | — | P49951 |
| Z | — | protein | 8 | — | — |
Compared structures
- 3GD1 · Structure of an Arrestin/Clathrin complex reveals a novel clathrin binding domain that… · the same entry in another collection · chain C against C, TM-score 1.00
- P49951 · AlphaFold monomer V2.0 prediction for clathrin heavy chain 1 (P49951) · a predicted model of the same protein · chain I against A, TM-score 0.99
- P17870 · AlphaFold monomer V2.0 prediction for beta-arrestin-1 (P17870) · a predicted model of the same protein · chain C against A, TM-score 0.98
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 P17870
- Every structure of UniProt P49951
- Elsewhere: RCSB PDB 3GD1 · PDBe 3GD1 · UniProt P17870 · UniProt P49951
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