Research workbench
Crystal structure of T. maritima 4-alpha-glucanotransferase
Analyse Crystal structure of T. maritima 4-alpha-glucanotransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1LWH
- Type
- protein
- Length
- 882 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 4-alpha-glucanotransferase
- EC
- 2.4.1.25
- UniProt
- P80099
- Ligands
- CA
- Pockets
- 9 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | 4-alpha-glucanotransferase (EC 2.4.1.25) | protein | 441 | 34% helix, 20% strand | P80099 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 825 | 0.76 | 0.80 | 70 | empty |
| 2 | 791 | 0.75 | 0.79 | 67 | empty |
| 3 | 91 | 0.54 | 0.84 | 18 | empty |
| 4 | 68 | 0.35 | 0.77 | 18 | empty |
| 5 | 84 | 0.34 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1312 Ų buried · 16 hydrogen bonds · protein-protein
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 P80099
- Elsewhere: RCSB PDB 1LWH · PDBe 1LWH · UniProt P80099
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.