1IB4
Crystal Structure of Polygalacturonase from Aspergillus Aculeatus at Ph4.5
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004650 | molecular_function | polygalacturonase activity |
A | 0005576 | cellular_component | extracellular region |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
A | 0045490 | biological_process | pectin catabolic process |
A | 0047911 | molecular_function | galacturan 1,4-alpha-galacturonidase activity |
A | 0071555 | biological_process | cell wall organization |
B | 0004650 | molecular_function | polygalacturonase activity |
B | 0005576 | cellular_component | extracellular region |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
B | 0045490 | biological_process | pectin catabolic process |
B | 0047911 | molecular_function | galacturan 1,4-alpha-galacturonidase activity |
B | 0071555 | biological_process | cell wall organization |
Functional Information from PROSITE/UniProt
site_id | PS00502 |
Number of Residues | 14 |
Details | POLYGALACTURONASE Polygalacturonase active site. GgyCsgGHGLs.IGS |
Chain | Residue | Details |
A | GLY195-SER208 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 60 |
Details | Repeat: {"description":"PbH1 1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 42 |
Details | Repeat: {"description":"PbH1 2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 40 |
Details | Repeat: {"description":"PbH1 3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 42 |
Details | Repeat: {"description":"PbH1 4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 44 |
Details | Repeat: {"description":"PbH1 5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"11518536","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | Active site: {"evidences":[{"source":"PubMed","id":"11518536","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | Glycosylation: {"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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 16 |
Details | Glycosylation: {"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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | Glycosylation: {"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"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1czf |
Chain | Residue | Details |
A | ASP181 | |
A | ASP180 | |
A | ASP159 | |
A | HIS202 |
site_id | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1czf |
Chain | Residue | Details |
B | ASP181 | |
B | ASP180 | |
B | ASP159 | |
B | HIS202 |