Research workbench
Pgld from campylobacter jejuni, nctc 11168, in complex with acetyl coenzyme a
Analyse Pgld from campylobacter jejuni, nctc 11168, 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
- 3BSY
- Type
- protein
- Length
- 581 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyltransferase
- EC
- 2.7.7.23
- UniProt
- Q0P9D1
- Ligands
- ACO
- Pockets
- 6 · best druggability 0.60
Structure
x-ray diffraction · 2 distinct chains · 13% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetyltransferase (EC 2.7.7.23) | protein | 193 | 13% helix, 28% strand | Q0P9D1 |
| B, C | Acetyltransferase (EC 2.7.7.23) | protein | 194 | 13% helix, 28% strand | Q0P9D1 |
Ligands and binding sites
- ACO · Acetyl coenzyme *A · ligand · 3 copies · chains A, C, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 249 | 0.60 | 0.80 | 37 | empty |
| 2 | 177 | 0.52 | 0.78 | 28 | empty |
| 3 | 152 | 0.49 | 0.78 | 27 | empty |
| 4 | 51 | 0.41 | 0.82 | 16 | empty |
| 5 | 51 | 0.40 | 0.81 | 15 | empty |
Interfaces
3 interfaces between chains.
- B–C · 817 Ų buried · 6 hydrogen bonds · protein-protein
- A–C · 792 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 760 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 3BSY · PglD from Campylobacter jejuni, NCTC 11168, in complex with acetyl coenzyme A · the same entry in another collection · chain A against A, TM-score 1.00
- Q0P9D1 · AlphaFold monomer V2.0 prediction for udp-N-acetylbacillosamine N-acetyltransferase… · 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 Q0P9D1
- Elsewhere: RCSB PDB 3BSY · PDBe 3BSY · UniProt Q0P9D1
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.