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 | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:11518536 |
| Chain | Residue | Details |
| A | ASP180 | |
| B | ASP180 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:11518536 |
| Chain | Residue | Details |
| A | HIS202 | |
| B | HIS202 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | CARBOHYD: O-linked (Man...) threonine => ECO:0000269|PubMed:11518536, ECO:0007744|PDB:1IA5, ECO:0007744|PDB:1IB4 |
| Chain | Residue | Details |
| A | THR5 | |
| A | THR24 | |
| B | THR5 | |
| B | THR24 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | CARBOHYD: O-linked (Man...) serine => ECO:0000269|PubMed:11518536, ECO:0007744|PDB:1IA5, ECO:0007744|PDB:1IB4 |
| Chain | Residue | Details |
| A | SER7 | |
| B | SER9 | |
| B | SER13 | |
| B | SER14 | |
| B | SER16 | |
| B | SER18 | |
| B | SER23 | |
| B | SER34 | |
| A | SER9 | |
| A | SER13 | |
| A | SER14 | |
| A | SER16 | |
| A | SER18 | |
| A | SER23 | |
| A | SER34 | |
| B | SER7 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11518536, ECO:0007744|PDB:1IA5, ECO:0007744|PDB:1IB4 |
| Chain | Residue | Details |
| A | ASN219 | |
| B | ASN219 |
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 |
