Research workbench
The GDP complex of the aminoglycoside 2'-phosphotransfere-iiia F108L mutant
Analyse The GDP complex of the aminoglycoside 2'-phosphotransfere-iiia F108L mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3TDW
- Type
- protein
- Length
- 302 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Gentamicin resistance protein
- UniProt
- P96762
- Ligands
- GDP, MG
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 55% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Gentamicin resistance protein | protein | 302 | 55% helix, 16% strand | P96762 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 670 | 0.69 | 0.77 | 57 | GDP, MG |
| 2 | 109 | 0.38 | 0.75 | 24 | empty |
| 3 | 87 | 0.33 | 0.74 | 17 | MG |
Compared structures
- 3TDW · The GDP complex of the aminoglycoside 2'-phosphotransfere-IIIa F108L mutant · 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 P96762
- Elsewhere: RCSB PDB 3TDW · PDBe 3TDW · UniProt P96762
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