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2XZK

THE ASPERGILLUS FUMIGATUS SIALIDASE IS A KDNASE: STRUCTURAL AND MECHANISTIC INSIGHTS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004308molecular_functionexo-alpha-sialidase activity
A0005737cellular_componentcytoplasm
A0006689biological_processganglioside catabolic process
A0009313biological_processoligosaccharide catabolic process
A0016020cellular_componentmembrane
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
B0004308molecular_functionexo-alpha-sialidase activity
B0005737cellular_componentcytoplasm
B0006689biological_processganglioside catabolic process
B0009313biological_processoligosaccharide catabolic process
B0016020cellular_componentmembrane
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0043231cellular_componentintracellular membrane-bounded organelle
B0052794molecular_functionexo-alpha-(2->3)-sialidase activity
B0052795molecular_functionexo-alpha-(2->6)-sialidase activity
B0052796molecular_functionexo-alpha-(2->8)-sialidase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:21247893
ChainResidueDetails
AARG59
BARG59
BARG78
BASP84
BGLN148
BARG265
BARG322
BLYS337
BTYR358
BASP376
AARG78
AASP84
AGLN148
AARG265
AARG322
ALYS337
ATYR358
AASP376

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ATYR331
BTYR331

site_idSWS_FT_FI3
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN235
AASN396
BASN235
BASN396

222036

PDB entries from 2024-07-03

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