Research workbench
Crystal structure of multiple sugar binding transport ATP- binding protein
Analyse Crystal structure of multiple sugar binding transport ATP- binding protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2D62
- Type
- protein
- Length
- 375 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Multiple sugar-binding transport ATP-binding protein
- UniProt
- O57933
- Ligands
- POP, SO4
- Pockets
- 2 · best druggability 0.46
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Multiple sugar-binding transport ATP-binding protein | protein | 375 | 30% helix, 34% strand | O57933 |
Ligands and binding sites
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 | 121 | 0.46 | 0.78 | 26 | empty |
| 2 | 59 | 0.27 | 0.73 | 12 | empty |
Modifications
Observed in the structure: 14 modified (engineered).
Compared structures
- 2D62 · Crystal structure of multiple sugar binding transport ATP-binding protein · 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 O57933
- Elsewhere: RCSB PDB 2D62 · PDBe 2D62 · UniProt O57933
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.