Research workbench
Molecular basis for cohesin acetylation by establishment of sister chromatid cohesion N-acetyltransferase ESCO1
Analyse Molecular basis for cohesin acetylation by establishment of sister chromatid… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5T53
- Type
- protein
- Length
- 187 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acetyltransferase ESCO1
- EC
- 2.3.1.-
- UniProt
- Q5FWF5
- Ligands
- ACO, ZN
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetyltransferase ESCO1 (EC 2.3.1.-) | protein | 187 | 33% helix, 27% strand | Q5FWF5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 347 | 0.67 | 0.81 | 37 | ACO |
| 2 | 78 | 0.36 | 0.76 | 18 | empty |
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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