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3NSX

The crystal structure of the The crystal structure of the D420A mutant of the alpha-glucosidase (FAMILY 31) from Ruminococcus obeum ATCC 29174

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0030246molecular_functioncarbohydrate binding
B0003824molecular_functioncatalytic activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0030246molecular_functioncarbohydrate binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE TRS A 664
ChainResidue
ATRP341
AHOH786
AHOH1023
AHOH1266
BTRP271
BPHE314

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE TRS A 665
ChainResidue
AHOH1068
ATRP169
AASP197
AASP307

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE TRS B 664
ChainResidue
APHE314
BTRP341
BHOH1055

Functional Information from PROSITE/UniProt
site_idPS00129
Number of Residues8
DetailsGLYCOSYL_HYDROL_F31_1 Glycosyl hydrolases family 31 active site. GFWnDMNE
ChainResidueDetails
AGLY303-GLU310

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PDB entries from 2024-09-11

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