Research workbench
Solution structure of helix-ring domain of cbl-B in the TYR363 phosphorylated form
Analyse Solution structure of helix-ring domain of cbl-B in the TYR363 phosphorylated… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LDR
- Type
- protein
- Length
- 82 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase cbl-B
- EC
- 6.3.2.-
- UniProt
- Q13191
- Ligands
- ZN
Structure
solution nmr · 1 distinct chain · 20% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase cbl-B (EC 6.3.2.-) | protein | 82 | 20% helix, 20% strand | Q13191 |
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.
Modifications
Observed in the structure: 1 disulfide, 1 modified (disulfide, phosphorylation).
Compared structures
- 2LDR · Solution structure of Helix-RING domain of Cbl-b in the Tyr363 phosphorylated form · the same entry in another collection · chain A against A, TM-score 1.00
- Q13191 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase cbl-B (Q13191) · a predicted model of the same protein · chain A against A, TM-score 0.84
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 Q13191
- Elsewhere: RCSB PDB 2LDR · PDBe 2LDR · UniProt Q13191
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