Research workbench
The crystal structure of isomaltulose synthase from erwinia rhapontici NX5
Analyse The crystal structure of isomaltulose synthase from erwinia rhapontici NX5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4HOW
- Type
- protein
- Length
- 559 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sucrose isomerase
- EC
- 5.4.99.11
- UniProt
- D9MPF2
- Ligands
- CA
- Pockets
- 7 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sucrose isomerase (EC 5.4.99.11) | protein | 559 | 33% helix, 18% strand | D9MPF2 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 67 | 0.74 | 0.98 | 19 | GOL |
| 2 | 202 | 0.61 | 0.82 | 20 | empty |
| 3 | 101 | 0.40 | 0.77 | 24 | empty |
| 4 | 72 | 0.34 | 0.76 | 18 | empty |
| 5 | 60 | 0.31 | 0.76 | 18 | empty |
Compared structures
- 4HOW · The crystal structure of isomaltulose synthase from Erwinia rhapontici NX5 · 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 D9MPF2
- Elsewhere: RCSB PDB 4HOW · PDBe 4HOW · UniProt D9MPF2
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