Research workbench
D domain of B-trcp
Analyse D domain of B-trcp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2P64
- Type
- protein
- Length
- 103 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- F-BOX/WD repeat protein 1A
- UniProt
- Q9Y297
- Ligands
- CD
Structure
x-ray diffraction · 2 distinct chains · 81% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | F-BOX/WD repeat protein 1A | protein | 51 | 78% helix, 0% strand | Q9Y297 |
| B | F-BOX/WD repeat protein 1A | protein | 52 | 83% helix, 0% strand | Q9Y297 |
Ligands and binding sites
- CD · Cadmium ion · metal · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 2053 Ų buried · 14 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
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 Q9Y297
- Elsewhere: RCSB PDB 2P64 · PDBe 2P64 · UniProt Q9Y297
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