Research workbench
Human ESCO1 (ECO1/CTF7 ortholog), acetyltransferase domain in complex with acetyl-CoA
Analyse Human ESCO1 (ECO1/CTF7 ortholog), acetyltransferase domain in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4MXE
- Type
- protein
- Length
- 356 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-acetyltransferase ESCO1
- EC
- 2.3.1.-
- UniProt
- Q5FWF5
- Ligands
- ACO
- Pockets
- 4 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 23% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-acetyltransferase ESCO1 (EC 2.3.1.-) | protein | 179 | 22% helix, 39% strand | Q5FWF5 |
| B | N-acetyltransferase ESCO1 (EC 2.3.1.-) | protein | 177 | 23% helix, 46% strand | Q5FWF5 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 315 | 0.63 | 0.79 | 34 | ACO |
| 2 | 296 | 0.60 | 0.78 | 29 | ACO |
| 3 | 110 | 0.44 | 0.78 | 20 | empty |
| 4 | 51 | 0.31 | 0.77 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 863 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 4MXE · Human ESCO1 (Eco1/Ctf7 ortholog), acetyltransferase domain in complex with acetyl-CoA · 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 0.90
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 4MXE · PDBe 4MXE · UniProt Q5FWF5
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