Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

5DGQ

Crystal structure of GH9 exo-beta-D-glucosaminidase PBPRA0520

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0008810molecular_functioncellulase activity
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0000272biological_processpolysaccharide catabolic process
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0008810molecular_functioncellulase activity
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue NA A 601
ChainResidue
AMET213
AASP241
AGLN243
AGLN248
ATYR301
AHOH941
AHOH1070

site_idAC2
Number of Residues7
Detailsbinding site for residue NA B 601
ChainResidue
BGLN243
BGLN248
BTYR301
BHOH988
BHOH996
BMET213
BASP241

247536

PDB entries from 2026-01-14

PDB statisticsPDBj update infoContact PDBjnumon