MolNFT v1 · #19354 · protein
Chloramphenicol phosphotransferase from streptomyces venezuelae in complex with atpgammas and chloramphenicol
1QHY: “Chloramphenicol phosphotransferase from streptomyces venezuelae in complex with atpgammas and chloramphenicol”. X-ray diffraction, 4 ligands (CLM, AGS, MG), 1 pocket (best druggability 0.67). MolNFT v1 #19354 on GenesisL1: 3D…
- PDB
- 1QHY
- Type
- protein
- Length
- 178 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chloramphenicol phosphotransferase
- EC
- 2.7.1.-
- UniProt
- Q56148
- Ligands
- CLM, AGS, MG, SO4
- Pockets
- 1 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chloramphenicol phosphotransferase (EC 2.7.1.-) | protein | 178 | 46% helix, 19% strand | Q56148 |
Ligands and binding sites
- CLM · Chloramphenicol · ligand · 2 copies · chains A
- AGS · Phosphothiophosphoric acid-adenylate ester · ligand · chains A
- MG · Magnesium ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 268 | 0.67 | 0.83 | 41 | MG, AGS, CLM |
Compared structures
- 1QHY · Chloramphenicol phosphotransferase from streptomyces venezuelae in complex with atpgammas… · the same entry in another collection · chain A against A, TM-score 1.00
- Q56148 · AlphaFold monomer V2.0 prediction for chloramphenicol 3-O phosphotransferase (Q56148) · 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 Q56148
- Elsewhere: RCSB PDB 1QHY · PDBe 1QHY · UniProt Q56148
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