Research workbench
Crystal structure of the AMP-bound complex of spectinomycin phosphotransferase, APH(9)-ia
Analyse Crystal structure of the AMP-bound complex of spectinomycin phosphotransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3I0Q
- Type
- protein
- Length
- 316 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Spectinomycin phosphotransferase
- UniProt
- O06916
- Ligands
- AMP, NI
- Pockets
- 4 · best druggability 0.59
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Spectinomycin phosphotransferase | protein | 316 | 42% helix, 10% strand | O06916 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 289 | 0.59 | 0.78 | 39 | empty |
| 2 | 184 | 0.57 | 0.80 | 25 | AMP |
| 3 | 94 | 0.40 | 0.77 | 21 | empty |
| 4 | 52 | 0.31 | 0.76 | 11 | empty |
Compared structures
- 3I0Q · Crystal Structure of the AMP-bound complex of Spectinomycin Phosphotransferase, APH(9)-Ia · the same entry in another collection · 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 O06916
- Elsewhere: RCSB PDB 3I0Q · PDBe 3I0Q · UniProt O06916
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