MolNFT v1 · #136883 · protein
Cryoem structure of the erad-associated E3 ubiquitin-protein ligase HRD1
5V6P: “Cryoem structure of the erad-associated E3 ubiquitin-protein ligase HRD1”. Electron microscopy. MolNFT v1 #136883 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5V6P
- Type
- protein
- Length
- 540 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q08109
Structure
electron microscopy · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 270 | — | Q08109 |
Compared structures
- 5V6P · CryoEM structure of the ERAD-associated E3 ubiquitin-protein ligase HRD1 · the same entry in another collection · chain A against A, TM-score 1.00
- Q08109 · AlphaFold monomer V2.0 prediction for erad-associated E3 ubiquitin- protein ligase HRD1… · a predicted model of the same protein · chain A against A, TM-score 0.93
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 Q08109
- Elsewhere: RCSB PDB 5V6P · PDBe 5V6P · UniProt Q08109
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