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1O7D

The structure of the bovine lysosomal a-mannosidase suggests a novel mechanism for low pH activation

Functional Information from GO Data
ChainGOidnamespacecontents
A0004559molecular_functionalpha-mannosidase activity
A0005975biological_processcarbohydrate metabolic process
A0006013biological_processmannose metabolic process
B0004559molecular_functionalpha-mannosidase activity
B0005975biological_processcarbohydrate metabolic process
B0006013biological_processmannose metabolic process
C0003824molecular_functioncatalytic activity
C0004559molecular_functionalpha-mannosidase activity
C0005975biological_processcarbohydrate metabolic process
C0006013biological_processmannose metabolic process
C0030246molecular_functioncarbohydrate binding
D0003824molecular_functioncatalytic activity
D0004559molecular_functionalpha-mannosidase activity
D0005975biological_processcarbohydrate metabolic process
D0006013biological_processmannose metabolic process
D0030246molecular_functioncarbohydrate binding
E0003824molecular_functioncatalytic activity
E0005975biological_processcarbohydrate metabolic process
E0030246molecular_functioncarbohydrate binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
EASN930
DASN692
DASN766

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASP74
AASP196
DASN651

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12634058, ECO:0007744|PDB:1O7D
ChainResidueDetails
AASN133

219869

PDB entries from 2024-05-15

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