Research workbench
4,6-alpha-glucanotransferase gtfb from limosilactobacillus reuteri ncc 2613
Analyse 4,6-alpha-glucanotransferase gtfb from limosilactobacillus reuteri ncc 2613 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7P38
- Type
- protein
- Length
- 1,662 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Dextransucrase
- EC
- 2.4.1.5
- UniProt
- A0A1Z2RUH3
- Ligands
- CA, SO4
- Pockets
- 17 · best druggability 0.85
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Dextransucrase (EC 2.4.1.5) | protein | 832 | 30% helix, 19% strand | A0A1Z2RUH3 |
| B | Dextransucrase (EC 2.4.1.5) | protein | 830 | 30% helix, 19% strand | A0A1Z2RUH3 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
- GOL · Glycerol · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
17 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1200 | 0.85 | 0.86 | 102 | empty |
| 2 | 1075 | 0.76 | 0.78 | 95 | GOL |
| 3 | 189 | 0.55 | 0.79 | 30 | empty |
| 4 | 258 | 0.51 | 0.75 | 38 | SO4 |
| 5 | 218 | 0.49 | 0.75 | 27 | empty |
Interfaces
1 interface between chains.
- A–B · 1334 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 7P38 · 4,6-alpha-glucanotransferase GtfB from Limosilactobacillus reuteri NCC 2613 · 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 A0A1Z2RUH3
- Elsewhere: RCSB PDB 7P38 · PDBe 7P38 · UniProt A0A1Z2RUH3
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