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

8K7K

Crystal structure of human lysosomal alpha-galactosidase A in complex with (2R,3S,4R,5R)-2,5-bis(hydroxymethyl)-1-methylpyrrolidine-3,4-diol

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0004557molecular_functionalpha-galactosidase activity
A0005102molecular_functionsignaling receptor binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005764cellular_componentlysosome
A0005794cellular_componentGolgi apparatus
A0005975biological_processcarbohydrate metabolic process
A0006629biological_processlipid metabolic process
A0009311biological_processoligosaccharide metabolic process
A0016020cellular_componentmembrane
A0016139biological_processglycoside catabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0016936molecular_functiongalactoside binding
A0019915biological_processlipid storage
A0030168biological_processplatelet activation
A0030431biological_processsleep
A0031133biological_processregulation of axon diameter
A0035578cellular_componentazurophil granule lumen
A0042803molecular_functionprotein homodimerization activity
A0043202cellular_componentlysosomal lumen
A0045019biological_processnegative regulation of nitric oxide biosynthetic process
A0046477biological_processglycosylceramide catabolic process
A0046479biological_processglycosphingolipid catabolic process
A0051001biological_processnegative regulation of nitric-oxide synthase activity
A0070062cellular_componentextracellular exosome
A0070527biological_processplatelet aggregation
A0090325biological_processregulation of locomotion involved in locomotory behavior
B0003824molecular_functioncatalytic activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0004557molecular_functionalpha-galactosidase activity
B0005102molecular_functionsignaling receptor binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0005764cellular_componentlysosome
B0005794cellular_componentGolgi apparatus
B0005975biological_processcarbohydrate metabolic process
B0006629biological_processlipid metabolic process
B0009311biological_processoligosaccharide metabolic process
B0016020cellular_componentmembrane
B0016139biological_processglycoside catabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0016936molecular_functiongalactoside binding
B0019915biological_processlipid storage
B0030168biological_processplatelet activation
B0030431biological_processsleep
B0031133biological_processregulation of axon diameter
B0035578cellular_componentazurophil granule lumen
B0042803molecular_functionprotein homodimerization activity
B0043202cellular_componentlysosomal lumen
B0045019biological_processnegative regulation of nitric oxide biosynthetic process
B0046477biological_processglycosylceramide catabolic process
B0046479biological_processglycosphingolipid catabolic process
B0051001biological_processnegative regulation of nitric-oxide synthase activity
B0070062cellular_componentextracellular exosome
B0070527biological_processplatelet aggregation
B0090325biological_processregulation of locomotion involved in locomotory behavior
Functional Information from PROSITE/UniProt
site_idPS00512
Number of Residues17
DetailsALPHA_GALACTOSIDASE Alpha-galactosidase signature. GYeyLcIDDc.Wmapq...RD
ChainResidueDetails
AGLY85-ASP101

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000250
ChainResidueDetails
AASP170
BASP170

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
AASP231
BASP231

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AGLU203
BGLU203

site_idSWS_FT_FI4
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15003450
ChainResidueDetails
AASN139
AASN192
BASN139
BASN192

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:15003450, ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN215
BASN215

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon