Research workbench
Pgld-CoA complex: an acetyl transferase from campylobacter jejuni
Analyse Pgld-CoA complex: an acetyl transferase from campylobacter jejuni in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VHE
- Type
- protein
- Length
- 375 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Acetyltransferase
- EC
- 2.7.7.23
- UniProt
- Q0P9D1
- Ligands
- COA, SO4
Structure
x-ray diffraction · 2 distinct chains · 14% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Acetyltransferase (EC 2.7.7.23) | protein | 194 | 13% helix, 28% strand | Q0P9D1 |
| B | Acetyltransferase (EC 2.7.7.23) | protein | 181 | 14% helix, 30% strand | Q0P9D1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2VHE · PglD-CoA complex: An acetyl transferase from Campylobacter jejuni · 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 1.00
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 2VHE · PDBe 2VHE · UniProt Q0P9D1
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