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1X0C

Improved Crystal Structure of Isopullulanase from Aspergillus niger ATCC 9642

Functional Information from GO Data
ChainGOidnamespacecontents
A0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
A0005576cellular_componentextracellular region
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0051675molecular_functionisopullulanase activity
B0004553molecular_functionhydrolase activity, hydrolyzing O-glycosyl compounds
B0005576cellular_componentextracellular region
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0051675molecular_functionisopullulanase activity
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DLNNGKQITvtDF
ChainResidueDetails
AASP514-PHE526

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues26
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
AASN24
AASN460
AASN491
AASN503
AASN535
BASN24
BASN94
BASN115
BASN138
BASN210
BASN305
AASN94
BASN381
BASN448
BASN455
BASN460
BASN491
BASN503
BASN535
AASN115
AASN138
AASN210
AASN305
AASN381
AASN448
AASN455

site_idSWS_FT_FI2
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN186
AASN486
BASN186
BASN486

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PDB entries from 2024-05-01

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