Research workbench
Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol
Analyse Catalytic domain of glucoamylase from aspergillus niger complexed with tris and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EQA
- Type
- protein
- Length
- 458 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P69328
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 458 | — | P69328 |
Compared structures
- 3EQA · Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol · the same entry in another collection · chain A against A, TM-score 1.00
- P69328 · AlphaFold monomer V2.0 prediction for glucoamylase (P69328) · 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 P69328
- Elsewhere: RCSB PDB 3EQA · PDBe 3EQA · UniProt P69328
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