Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1EUT

SIALIDASE, LARGE 68KD FORM, COMPLEXED WITH GALACTOSE

Functional Information from GO Data
ChainGOidnamespacecontents
A0004308molecular_functionexo-alpha-sialidase activity
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005975biological_processcarbohydrate metabolic process
A0006689biological_processganglioside catabolic process
A0008152biological_processmetabolic process
A0009313biological_processoligosaccharide catabolic process
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0043231cellular_componentintracellular membrane-bounded organelle
A0052794molecular_functionexo-alpha-(2->3)-sialidase activity
A0052795molecular_functionexo-alpha-(2->6)-sialidase activity
A0052796molecular_functionexo-alpha-(2->8)-sialidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 1
ChainResidue
AASN528
AASP531
AASN533
ATHR536
AALA639
AGLU640

site_idACT
Number of Residues9
DetailsACTIVE SITE. SITE INCLUDES TWO CONTACTS WITH SYMMETRY-RELATED MOLECULES.
ChainResidue
AGLN224
AGLY245
AALA250
AGLY292
AASN311
APHE318
AALA619
ATYR635
AALA637

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250
ChainResidueDetails
AASP92

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000255
ChainResidueDetails
AGLU260

site_idSWS_FT_FI3
Number of Residues1
DetailsACT_SITE: Nucleophile
ChainResidueDetails
ATYR370

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
AARG68
AARG276

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 835
ChainResidueDetails
AASP92activator, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
AGLU260activator, increase nucleophilicity, promote heterolysis, proton acceptor, proton donor
ATYR370covalently attached, nucleofuge, nucleophile, proton acceptor, proton donor

217705

PDB entries from 2024-03-27

PDB statisticsPDBj update infoContact PDBjnumon