Research workbench
Solution structure of ring domain of E3 ubiquitin ligase DOA10
Analyse Solution structure of ring domain of E3 ubiquitin ligase DOA10 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2M6M
- Type
- protein
- Length
- 83 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Erad-associated E3 ubiquitin-protein ligase DOA10
- EC
- 6.3.2.-
- UniProt
- P40318
- Ligands
- ZN
Structure
solution nmr · 1 distinct chain · 12% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Erad-associated E3 ubiquitin-protein ligase DOA10 (EC 6.3.2.-) | protein | 83 | 12% helix, 7% strand | P40318 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2M6M · Solution structure of RING domain of E3 ubiquitin ligase Doa10 · the same entry in another collection · chain A against A, TM-score 1.00
- P40318 · AlphaFold monomer V2.0 prediction for erad-associated E3 ubiquitin- protein ligase DOA10… · a predicted model of the same protein · chain A against A, TM-score 0.71
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 P40318
- Elsewhere: RCSB PDB 2M6M · PDBe 2M6M · UniProt P40318
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