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2IQ7

Crystal structure of the polygalacturonase from Colletotrichum lupini and its implications for the interaction with polygalacturonase-inhibiting proteins

Functional Information from GO Data
ChainGOidnamespacecontents
A0004650molecular_functionpolygalacturonase activity
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0045490biological_processpectin catabolic process
A0071555biological_processcell wall organization
B0004650molecular_functionpolygalacturonase activity
B0005975biological_processcarbohydrate metabolic process
B0016798molecular_functionhydrolase activity, acting on glycosyl bonds
B0045490biological_processpectin catabolic process
B0071555biological_processcell wall organization
C0004650molecular_functionpolygalacturonase activity
C0005975biological_processcarbohydrate metabolic process
C0016798molecular_functionhydrolase activity, acting on glycosyl bonds
C0045490biological_processpectin catabolic process
C0071555biological_processcell wall organization
D0004650molecular_functionpolygalacturonase activity
D0005975biological_processcarbohydrate metabolic process
D0016798molecular_functionhydrolase activity, acting on glycosyl bonds
D0045490biological_processpectin catabolic process
D0071555biological_processcell wall organization
E0004650molecular_functionpolygalacturonase activity
E0005975biological_processcarbohydrate metabolic process
E0016798molecular_functionhydrolase activity, acting on glycosyl bonds
E0045490biological_processpectin catabolic process
E0071555biological_processcell wall organization
F0004650molecular_functionpolygalacturonase activity
F0005975biological_processcarbohydrate metabolic process
F0016798molecular_functionhydrolase activity, acting on glycosyl bonds
F0045490biological_processpectin catabolic process
F0071555biological_processcell wall organization
G0004650molecular_functionpolygalacturonase activity
G0005975biological_processcarbohydrate metabolic process
G0016798molecular_functionhydrolase activity, acting on glycosyl bonds
G0045490biological_processpectin catabolic process
G0071555biological_processcell wall organization
Functional Information from PROSITE/UniProt
site_idPS00502
Number of Residues14
DetailsPOLYGALACTURONASE Polygalacturonase active site. GgtCsgGHGLs.IGS
ChainResidueDetails
AGLY214-SER227

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1czf
ChainResidueDetails
AHIS221
AASP199
AASP200
AASP178

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1czf
ChainResidueDetails
BHIS221
BASP199
BASP200
BASP178

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1czf
ChainResidueDetails
CHIS221
CASP199
CASP200
CASP178

site_idCSA4
Number of Residues4
DetailsAnnotated By Reference To The Literature 1czf
ChainResidueDetails
DHIS221
DASP199
DASP200
DASP178

site_idCSA5
Number of Residues4
DetailsAnnotated By Reference To The Literature 1czf
ChainResidueDetails
EHIS221
EASP199
EASP200
EASP178

site_idCSA6
Number of Residues4
DetailsAnnotated By Reference To The Literature 1czf
ChainResidueDetails
FHIS221
FASP199
FASP200
FASP178

site_idCSA7
Number of Residues4
DetailsAnnotated By Reference To The Literature 1czf
ChainResidueDetails
GHIS221
GASP199
GASP200
GASP178

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PDB entries from 2024-07-31

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