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Site directed mutations of the active site residue tyrosine 195 of cyclodextrin glyxosyltransferase from bacillus circulans strain 251 affecting activity and product specificity
Analyse Site directed mutations of the active site residue tyrosine 195 of cyclodextrin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1CGY
- Type
- protein
- Length
- 686 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P43379
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 686 | — | P43379 |
Compared structures
- 1CGY · Site directed mutations of the active site residue tyrosine 195 of cyclodextrin… · 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 1CGY · PDBe 1CGY · UniProt P43379
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