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Nucleotide sequence and X-ray structure of cyclodextrin glycosyltransferase from bacillus circulans strain 251 in a maltose- dependent crystal form
Analyse Nucleotide sequence and X-ray structure of cyclodextrin glycosyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CDG
- Type
- protein
- Length
- 686 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cyclodextrin glycosyl-transferase
- EC
- 2.4.1.19
- UniProt
- P43379
- Ligands
- GLC, CA
- Pockets
- 4 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cyclodextrin glycosyl-transferase (EC 2.4.1.19) | protein | 686 | 23% helix, 30% strand | P43379 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 6 copies · chains A
- CA · Calcium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 417 | 0.75 | 0.85 | 62 | empty |
| 2 | 423 | 0.64 | 0.78 | 34 | empty |
| 3 | 116 | 0.39 | 0.75 | 22 | empty |
| 4 | 85 | 0.37 | 0.77 | 18 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1CDG · Nucleotide sequence and X-ray structure of cyclodextrin glycosyltransferase from bacillus… · the same entry in another collection · chain A against A, TM-score 1.00
- P43379 · AlphaFold monomer V2.0 prediction for cyclomaltodextrin glucanotransferase (P43379) · a predicted model of the same protein · 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 P43379
- Elsewhere: RCSB PDB 1CDG · PDBe 1CDG · UniProt P43379
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