Research workbench
Crystal structure of MUCH37-HRPN13 ctd complex
Analyse Crystal structure of MUCH37-HRPN13 ctd complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4WLQ
- Type
- protein
- Length
- 391 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9WUP7, Q16186
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 292 | — | Q9WUP7 |
| B | — | protein | 99 | — | Q16186 |
Compared structures
- Q9WUP7 · AlphaFold monomer V2.0 prediction for ubiquitin carboxyl-terminal hydrolase isozyme L5… · a predicted model of the same protein · chain A against A, TM-score 0.96
- Q16186 · AlphaFold monomer V2.0 prediction for proteasomal ubiquitin receptor ADRM1 (Q16186) · a predicted model of the same protein · chain B against A, TM-score 0.70
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 Q9WUP7
- Every structure of UniProt Q16186
- Elsewhere: RCSB PDB 4WLQ · PDBe 4WLQ · UniProt Q9WUP7 · UniProt Q16186
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