7PM4

Cryo-EM structures of human fucosidase FucA1 reveal insight into substate recognition and catalysis.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004560	molecular_function	alpha-L-fucosidase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005737	cellular_component	cytoplasm
A	0005764	cellular_component	lysosome
A	0005975	biological_process	carbohydrate metabolic process
A	0006004	biological_process	fucose metabolic process
A	0006629	biological_process	lipid metabolic process
A	0016020	cellular_component	membrane
A	0016139	biological_process	glycoside catabolic process
A	0016787	molecular_function	hydrolase activity
A	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
A	0019377	biological_process	glycolipid catabolic process
A	0035578	cellular_component	azurophil granule lumen
A	0043202	cellular_component	lysosomal lumen
A	0070062	cellular_component	extracellular exosome
B	0004560	molecular_function	alpha-L-fucosidase activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005737	cellular_component	cytoplasm
B	0005764	cellular_component	lysosome
B	0005975	biological_process	carbohydrate metabolic process
B	0006004	biological_process	fucose metabolic process
B	0006629	biological_process	lipid metabolic process
B	0016020	cellular_component	membrane
B	0016139	biological_process	glycoside catabolic process
B	0016787	molecular_function	hydrolase activity
B	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
B	0019377	biological_process	glycolipid catabolic process
B	0035578	cellular_component	azurophil granule lumen
B	0043202	cellular_component	lysosomal lumen
B	0070062	cellular_component	extracellular exosome
C	0004560	molecular_function	alpha-L-fucosidase activity
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005737	cellular_component	cytoplasm
C	0005764	cellular_component	lysosome
C	0005975	biological_process	carbohydrate metabolic process
C	0006004	biological_process	fucose metabolic process
C	0006629	biological_process	lipid metabolic process
C	0016020	cellular_component	membrane
C	0016139	biological_process	glycoside catabolic process
C	0016787	molecular_function	hydrolase activity
C	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
C	0019377	biological_process	glycolipid catabolic process
C	0035578	cellular_component	azurophil granule lumen
C	0043202	cellular_component	lysosomal lumen
C	0070062	cellular_component	extracellular exosome
D	0004560	molecular_function	alpha-L-fucosidase activity
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005737	cellular_component	cytoplasm
D	0005764	cellular_component	lysosome
D	0005975	biological_process	carbohydrate metabolic process
D	0006004	biological_process	fucose metabolic process
D	0006629	biological_process	lipid metabolic process
D	0016020	cellular_component	membrane
D	0016139	biological_process	glycoside catabolic process
D	0016787	molecular_function	hydrolase activity
D	0016798	molecular_function	hydrolase activity, acting on glycosyl bonds
D	0019377	biological_process	glycolipid catabolic process
D	0035578	cellular_component	azurophil granule lumen
D	0043202	cellular_component	lysosomal lumen
D	0070062	cellular_component	extracellular exosome

Functional Information from PROSITE/UniProt

site_id	PS00385
Number of Residues	12
Details	ALPHA_L_FUCOSIDASE Alpha-L-fucosidase putative active site. PqsLpdhKWEmC

Chain	Residue	Details
A	PRO280-CYS291

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Site: {"description":"May be important for catalysis"}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	8
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---