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Structure of the catalytic domain of aspergillus niger glucoamylase

Analyse Structure of the catalytic domain of aspergillus niger glucoamylase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6FRV
Type: protein
Length: 467 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P69328
Ligands: NAG, MAN

Structure

x-ray diffraction · 1 distinct chain.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	467	—	P69328

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
MAN · alpha-D-mannopyranose · sugar · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

6FRV · Structure of the catalytic domain of Aspergillus niger Glucoamylase · 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 0.99

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 6FRV · PDBe 6FRV · UniProt P69328

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