Research workbench
NMR structure of the ring domain in ubiquitin ligase GP78
Analyse NMR structure of the ring domain in ubiquitin ligase GP78 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LXH
- Type
- protein
- Length
- 58 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase amfr
- EC
- 6.3.2.-
- UniProt
- Q9UKV5
- Ligands
- ZN
Structure
solution nmr · 1 distinct chain · 28% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | E3 ubiquitin-protein ligase amfr (EC 6.3.2.-) | protein | 58 | 28% helix, 10% strand | Q9UKV5 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2LXH · NMR structure of the RING domain in ubiquitin ligase gp78 · the same entry in another collection · chain C against C, TM-score 1.00
- Q9UKV5 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase amfr (Q9UKV5) · a predicted model of the same protein · chain C 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 Q9UKV5
- Elsewhere: RCSB PDB 2LXH · PDBe 2LXH · UniProt Q9UKV5
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