MolNFT v1 · #75867 · protein
Structure of the RTT109-ACCOA/VPS75 complex and implications for chaperone-mediated histone acetylation
3Q35: “Structure of the RTT109-ACCOA/VPS75 complex and implications for chaperone-mediated histone acetylation”. X-ray diffraction. MolNFT v1 #75867 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3Q35
- Type
- protein
- Length
- 607 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q07794, P53853
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 394 | — | Q07794 |
| B | — | protein | 213 | — | P53853 |
Compared structures
- 3Q35 · Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated… · the same entry in another collection · chain A against A, TM-score 1.00
- P53853 · AlphaFold monomer V2.0 prediction for vacuolar protein sorting- associated protein 75… · a predicted model of the same protein · chain B against A, TM-score 0.95
- Q07794 · AlphaFold monomer V2.0 prediction for histone acetyltransferase RTT109 (Q07794) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 Q07794
- Every structure of UniProt P53853
- Elsewhere: RCSB PDB 3Q35 · PDBe 3Q35 · UniProt Q07794 · UniProt P53853
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