Research workbench
Amylase in complex with branched ligand
Analyse Amylase in complex with branched ligand in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6GYA
- Type
- protein
- Length
- 1,924 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A3P8MUS3
- Ligands
- GLC, BGC, CA, NA
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 481 | — | A0A3P8MUS3 |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 24 copies · chains A, B, C, D
- BGC · beta-D-glucopyranose · sugar · 3 copies · chains B, C, D
- CA · Calcium ion · metal · 12 copies · chains A, B, C, D
- NA · Sodium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6GYA · Amylase in complex with branched ligand · 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 A0A3P8MUS3
- Elsewhere: RCSB PDB 6GYA · PDBe 6GYA · UniProt A0A3P8MUS3
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