MolNFT v1 · #134472 · protein
Molecular basis for cohesin acetylation by establishment of sister chromatid cohesion N-acetyltransferase ESCO1
5T53: “Molecular basis for cohesin acetylation by establishment of sister chromatid cohesion N-acetyltransferase…”. X-ray diffraction, 2 ligands (ACO, ZN). MolNFT v1 #134472 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5T53
- Type
- protein
- Length
- 187 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q5FWF5
- Ligands
- ACO, ZN
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 187 | — | Q5FWF5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5T53 · Molecular basis for cohesin acetylation by establishment of sister chromatid cohesion… · the same entry in another collection · chain A against A, TM-score 1.00
- Q5FWF5 · AlphaFold monomer V2.0 prediction for N-acetyltransferase ESCO1 (Q5FWF5) · a predicted model of the same protein · chain A against A, TM-score 0.89
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 Q5FWF5
- Elsewhere: RCSB PDB 5T53 · PDBe 5T53 · UniProt Q5FWF5
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