Research workbench
Active site metal depleted aldos-2-ulose dehydratase
Analyse Active site metal depleted aldos-2-ulose dehydratase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4A7Y
- Type
- protein
- Length
- 880 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aldos-2-ulose dehydratase
- EC
- 4.2.1.110
- UniProt
- P84193
- Ligands
- NHF, ZN, MG
- Pockets
- 9 · best druggability 0.71
Structure
x-ray diffraction · 1 distinct chain · 4% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aldos-2-ulose dehydratase (EC 4.2.1.110) | protein | 880 | 4% helix, 45% strand | P84193 |
Ligands and binding sites
- NHF · 1,5-anhydro-D-fructose · ligand · 2 copies · chains A
- ZN · Zinc ion · metal · chains A
- MG · Magnesium ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 698 | 0.71 | 0.78 | 61 | empty |
| 2 | 659 | 0.67 | 0.76 | 58 | NHF |
| 3 | 252 | 0.66 | 0.83 | 45 | empty |
| 4 | 293 | 0.61 | 0.79 | 32 | NHF |
| 5 | 275 | 0.55 | 0.76 | 30 | empty |
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 P84193
- Elsewhere: RCSB PDB 4A7Y · PDBe 4A7Y · UniProt P84193
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