Research workbench
Galactoside acetyltransferase in complex with acetyl-coenzyme a
Analyse Galactoside acetyltransferase in complex with acetyl-coenzyme a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KRR
- Type
- protein
- Length
- 600 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Galactoside O-acetyltransferase
- EC
- 2.3.1.18
- UniProt
- P07464
- Ligands
- ACO
- Pockets
- 3 · best druggability 0.83
Structure
x-ray diffraction · 1 distinct chain · 19% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Galactoside O-acetyltransferase (EC 2.3.1.18) | protein | 200 | 19% helix, 27% strand | P07464 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1008 | 0.83 | 0.84 | 108 | ACO |
| 2 | 741 | 0.78 | 0.82 | 71 | ACO |
| 3 | 767 | 0.76 | 0.80 | 71 | ACO |
Interfaces
3 interfaces between chains.
- A–C · 1604 Ų buried · 8 hydrogen bonds · protein-protein
- B–C · 1599 Ų buried · 7 hydrogen bonds · protein-protein
- A–B · 1562 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 1KRR · Galactoside Acetyltransferase in Complex with Acetyl-Coenzyme A · the same entry in another collection · chain A against A, TM-score 1.00
- P07464 · AlphaFold monomer V2.0 prediction for galactoside O-acetyltransferase (P07464) · a predicted model of the same protein · chain A against A, TM-score 0.99
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 P07464
- Elsewhere: RCSB PDB 1KRR · PDBe 1KRR · UniProt P07464
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