Research workbench
Crystal structure of ubiquitin-conjugating enzyme E2-25KDA (huntington interacting protein 2) M172A mutant
Analyse Crystal structure of ubiquitin-conjugating enzyme E2-25KDA (huntington… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3E46
- Type
- protein
- Length
- 202 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquitin-conjugating enzyme E2-25 kda
- EC
- 6.3.2.19
- UniProt
- P61086
- Ligands
- CA
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ubiquitin-conjugating enzyme E2-25 kda (EC 6.3.2.19) | protein | 202 | 46% helix, 13% strand | P61086 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3E46 · Crystal structure of ubiquitin-conjugating enzyme E2-25kDa (Huntington interacting… · the same entry in another collection · chain A against A, TM-score 1.00
- P61086 · AlphaFold monomer V2.0 prediction for ubiquitin-conjugating enzyme E2 K (P61086) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P61086
- Elsewhere: RCSB PDB 3E46 · PDBe 3E46 · UniProt P61086
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