Research workbench
Adaptor dependent degradation of a cell-cycle regulator reveals diversity in substrate architectures
Analyse Adaptor dependent degradation of a cell-cycle regulator reveals diversity in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3U2A
- Type
- protein
- Length
- 112 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ggdef family protein
- EC
- 3.1.4.52
- UniProt
- Q9A310
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ggdef family protein (EC 3.1.4.52) | protein | 112 | 31% helix, 34% strand | Q9A310 |
Modifications
Observed in the structure: 1 modified (oxidation).
Compared structures
- 3U2A · Adaptor dependent degradation of a cell-cycle regulator reveals diversity in substrate… · the same entry in another collection · chain A against A, TM-score 1.00
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 Q9A310
- Elsewhere: RCSB PDB 3U2A · PDBe 3U2A · UniProt Q9A310
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