Research workbench
Cyclic alpha-maltosyl-(1-->6)-maltose hydrolase from arthrobacter globiformis, complex with cyclic alpha-maltosyl-(1-->6)-maltose
Analyse Cyclic alpha-maltosyl-(1-->6)-maltose hydrolase from arthrobacter globiformis… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6A0J
- Type
- protein
- Length
- 442 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclic maltosyl-maltose hydrolase
- UniProt
- D2YYE1
- Ligands
- GLC, CA
- Pockets
- 1 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclic maltosyl-maltose hydrolase | protein | 442 | 38% helix, 19% strand | D2YYE1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 138 | 0.42 | 0.75 | 19 | GLC |
Compared structures
- 6A0J · Cyclic alpha-maltosyl-(1-->6)-maltose hydrolase from Arthrobacter globiformis, 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 D2YYE1
- Elsewhere: RCSB PDB 6A0J · PDBe 6A0J · UniProt D2YYE1
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