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1IB4

Crystal Structure of Polygalacturonase from Aspergillus Aculeatus at Ph4.5

Functional Information from GO Data
ChainGOidnamespacecontents
A0004650molecular_functionpolygalacturonase activity
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0016787molecular_functionhydrolase activity
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0045490biological_processpectin catabolic process
A0047911molecular_functiongalacturan 1,4-alpha-galacturonidase activity
A0071555biological_processcell wall organization
B0004650molecular_functionpolygalacturonase activity
B0005576cellular_componentextracellular region
B0005975biological_processcarbohydrate metabolic process
B0016787molecular_functionhydrolase activity
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0045490biological_processpectin catabolic process
B0047911molecular_functiongalacturan 1,4-alpha-galacturonidase activity
B0071555biological_processcell wall organization
Functional Information from PROSITE/UniProt
site_idPS00502
Number of Residues14
DetailsPOLYGALACTURONASE Polygalacturonase active site. GgyCsgGHGLs.IGS
ChainResidueDetails
AGLY195-SER208

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues60
DetailsRepeat: {"description":"PbH1 1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues42
DetailsRepeat: {"description":"PbH1 2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues40
DetailsRepeat: {"description":"PbH1 3","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues42
DetailsRepeat: {"description":"PbH1 4","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues44
DetailsRepeat: {"description":"PbH1 5","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"11518536","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"11518536","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsGlycosylation: {"description":"O-linked (Man...) threonine","evidences":[{"source":"PubMed","id":"11518536","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IA5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1IB4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues16
DetailsGlycosylation: {"description":"O-linked (Man...) serine","evidences":[{"source":"PubMed","id":"11518536","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IA5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1IB4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11518536","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1IA5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1IB4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1czf
ChainResidueDetails
AASP181
AASP180
AASP159
AHIS202

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1czf
ChainResidueDetails
BASP181
BASP180
BASP159
BHIS202

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PDB entries from 2025-08-27

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