Research workbench
Crystal structure of phosphopantetheine adenylyltransferase with ADP
Analyse Crystal structure of phosphopantetheine adenylyltransferase with ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1O6B
- Type
- protein
- Length
- 163 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Phosphopantetheine adenylyltransferase
- EC
- 2.7.7.3
- UniProt
- O34797
- Ligands
- ADP, MG, PO4, CL
- Pockets
- 1 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Phosphopantetheine adenylyltransferase (EC 2.7.7.3) | protein | 163 | 43% helix, 18% strand | O34797 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- MG · Magnesium ion · metal · chains A
- PO4 · Phosphate ion · ion · chains A
- CL · Chloride 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 | 487 | 0.71 | 0.81 | 56 | PO4, ADP |
Modifications
Observed in the structure: 3 modified (engineered).
Compared structures
- 1O6B · Crystal structure of phosphopantetheine adenylyltransferase with ADP · the same entry in another collection · chain A against A, TM-score 1.00
- O34797 · AlphaFold monomer V2.0 prediction for phosphopantetheine adenylyltransferase (O34797) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 O34797
- Elsewhere: RCSB PDB 1O6B · PDBe 1O6B · UniProt O34797
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