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Structure of first catalytic cysteine half-domain of mouse ubiquitin- activating enzyme
Analyse Structure of first catalytic cysteine half-domain of mouse ubiquitin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2V31
- Type
- protein
- Length
- 112 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquitin-activating enzyme E1 X
- UniProt
- Q02053
Structure
solution nmr · 1 distinct chain · 3% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ubiquitin-activating enzyme E1 X | protein | 112 | 3% helix, 29% strand | Q02053 |
Compared structures
- 2V31 · Structure of First Catalytic Cysteine Half-domain of mouse ubiquitin- activating enzyme · the same entry in another collection · chain A against A, TM-score 1.00
- Q02053 · AlphaFold monomer V2.0 prediction for ubiquitin-like modifier- activating enzyme 1… · a predicted model of the same protein · chain A against A, TM-score 0.68
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 Q02053
- Elsewhere: RCSB PDB 2V31 · PDBe 2V31 · UniProt Q02053
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