Research workbench
Crystal structure of glcv, the ABC-ATPase of the glucose ABC transporter from sulfolobus solfataricus
Analyse Crystal structure of glcv, the ABC-ATPase of the glucose ABC transporter from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OXU
- Type
- protein
- Length
- 1,059 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ABC transporter, ATP binding protein
- Ligands
- ADP, MG, IOD
- Pockets
- 7 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 28% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | ABC transporter, ATP binding protein | protein | 353 | 28% helix, 36% strand | — |
Ligands and binding sites
- ADP · Adenosine-5'-diphosphate · ligand · 3 copies · chains A, B, C
- MG · Magnesium ion · metal · 3 copies · chains A, B, C
- IOD · Iodide ion · ion · 60 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 103 | 0.60 | 0.86 | 23 | IOD |
| 2 | 237 | 0.53 | 0.76 | 34 | IOD |
| 3 | 256 | 0.51 | 0.75 | 32 | empty |
| 4 | 200 | 0.50 | 0.76 | 24 | IOD |
| 5 | 206 | 0.48 | 0.75 | 26 | IOD |
Interfaces
2 interfaces between chains.
- A–B · 185 Ų buried · 0 hydrogen bonds · protein-protein
- A–C · 173 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 1OXU · Crystal structure of GlcV, the ABC-ATPase of the glucose ABC transporter from Sulfolobus… · 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
- Elsewhere: RCSB PDB 1OXU · PDBe 1OXU
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