Research workbench
Hoxa complex of cyclodextrin glycosyltransferase mutant
Analyse Hoxa complex of cyclodextrin glycosyltransferase mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6CGT
- Type
- protein
- Length
- 684 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P30920
- Ligands
- DAG, OPG, GLC, CA
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 684 | — | P30920 |
Ligands and binding sites
- DAG · 4-amino-4,6-dideoxy-beta-D-glucopyranose · ligand · 2 copies · chains A
- OPG · Oxiranpseudoglucose · ligand · 2 copies · chains A
- GLC · alpha-D-glucopyranose · sugar · 2 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.
Compared structures
- 6CGT · Hoxa complex of cyclodextrin glycosyltransferase mutant · the same entry in another collection · chain A against A, TM-score 1.00
- P30920 · AlphaFold monomer V2.0 prediction for cyclomaltodextrin glucanotransferase (P30920) · 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 P30920
- Elsewhere: RCSB PDB 6CGT · PDBe 6CGT · UniProt P30920
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