Research workbench
Glge isoform 1 from streptomyces coelicolor with alpha-cyclodextrin bound
Analyse Glge isoform 1 from streptomyces coelicolor with alpha-cyclodextrin bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZST
- Type
- protein
- Length
- 1,298 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative glucanohydrolase PEP1A glge isoform 1
- EC
- 3.2.1.-, 2.4.1.-
- UniProt
- Q9L1K2
- Ligands
- GLC
- Pockets
- 8 · best druggability 0.70
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Putative glucanohydrolase PEP1A glge isoform 1 (EC 3.2.1.-, 2.4.1.-) | protein | 649 | 34% helix, 24% strand | Q9L1K2 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 12 copies · chains A, B
- EDO · 1,2-ethanediol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 270 | 0.70 | 0.85 | 41 | empty |
| 2 | 269 | 0.69 | 0.84 | 42 | empty |
| 3 | 171 | 0.47 | 0.76 | 28 | empty |
| 4 | 134 | 0.42 | 0.76 | 19 | empty |
| 5 | 82 | 0.39 | 0.78 | 20 | empty |
Compared structures
- 3ZST · GlgE isoform 1 from Streptomyces coelicolor with alpha-cyclodextrin bound · the same entry in another collection · chain A against A, TM-score 1.00
- Q9L1K2 · AlphaFold monomer V2.0 prediction for alpha-1,4-GLUCAN:MALTOSE-1-phosphate… · a predicted model of the same protein · chain B 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 Q9L1K2
- Elsewhere: RCSB PDB 3ZST · PDBe 3ZST · UniProt Q9L1K2
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