Research workbench
Yeast N-acetyltransferase MPR1 in complex with chop
Analyse Yeast N-acetyltransferase MPR1 in complex with chop in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3W6X
- Type
- protein
- Length
- 2,701 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- E9P8D2
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | — | protein | 226 | — | E9P8D2 |
| D, K | — | protein | 224 | — | E9P8D2 |
| E, G, H, I, J, L | — | protein | 225 | — | E9P8D2 |
| F | — | protein | 225 | — | E9P8D2 |
Compared structures
- 3W6X · Yeast N-acetyltransferase Mpr1 in complex with CHOP · the same entry in another collection · chain I against I, 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 E9P8D2
- Elsewhere: RCSB PDB 3W6X · PDBe 3W6X · UniProt E9P8D2
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