Research workbench
GET3 with ADP from D. hansenii in closed form
Analyse GET3 with ADP from D. hansenii in closed form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3IO3
- Type
- protein
- Length
- 230 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DEHA2D07832P
- UniProt
- Q6BSM0
- Ligands
- ADP, ZN, MG, NA
- Pockets
- 2 · best druggability 0.38
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DEHA2D07832P | protein | 230 | 40% helix, 20% strand | Q6BSM0 |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · chains A
- ZN · Zinc ion · metal · chains A
- MG · Magnesium ion · metal · chains A
- NA · Sodium ion · metal · chains A
- GOL · Glycerol · additive · 3 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 99 | 0.38 | 0.76 | 25 | ADP |
| 2 | 52 | 0.29 | 0.75 | 13 | GOL |
Compared structures
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 Q6BSM0
- Elsewhere: RCSB PDB 3IO3 · PDBe 3IO3 · UniProt Q6BSM0
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