Research workbench
Crystal structure analysis of sucrose HYDROLASE(SUH) E322Q-sucrose complex
Analyse Crystal structure analysis of sucrose HYDROLASE(SUH) E322Q-sucrose complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3CZK
- Type
- protein
- Length
- 618 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Sucrose hydrolase
- EC
- 3.2.1.48
- UniProt
- Q6UVM5
- Ligands
- GLC, FRU
- Pockets
- 5 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Sucrose hydrolase (EC 3.2.1.48) | protein | 618 | 43% helix, 16% strand | Q6UVM5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 353 | 0.75 | 0.86 | 51 | GLC, FRU |
| 2 | 110 | 0.45 | 0.79 | 18 | empty |
| 3 | 114 | 0.43 | 0.77 | 18 | empty |
| 4 | 105 | 0.42 | 0.78 | 22 | empty |
| 5 | 61 | 0.40 | 0.80 | 23 | empty |
Compared structures
- 3CZK · Crystal Structure Analysis of Sucrose hydrolase(SUH) E322Q-sucrose complex · 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 Q6UVM5
- Elsewhere: RCSB PDB 3CZK · PDBe 3CZK · UniProt Q6UVM5
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