Research workbench
Hsa-glucose complex
Analyse Hsa-glucose complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IW2
- Type
- protein
- Length
- 578 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serum albumin
- UniProt
- P02768
- Ligands
- GLO, GLC, PO4
- Pockets
- 6 · best druggability 0.86
Structure
x-ray diffraction · 1 distinct chain · 74% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serum albumin | protein | 578 | 74% helix, 0% strand | P02768 |
Ligands and binding sites
- GLO · D-glucose · sugar · chains A
- GLC · alpha-D-glucopyranose · sugar · chains A
- PO4 · Phosphate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1077 | 0.86 | 0.87 | 114 | GLO, GLC, PO4 |
| 2 | 57 | 0.70 | 0.97 | 18 | empty |
| 3 | 124 | 0.56 | 0.83 | 18 | empty |
| 4 | 192 | 0.54 | 0.78 | 25 | empty |
| 5 | 54 | 0.33 | 0.77 | 11 | empty |
Modifications
Observed in the structure: 17 disulfide, 1 glycan (disulfide, glycation).
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 P02768
- Elsewhere: RCSB PDB 4IW2 · PDBe 4IW2 · UniProt P02768
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