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1IA5

POLYGALACTURONASE FROM ASPERGILLUS ACULEATUS

Functional Information from GO Data
ChainGOidnamespacecontents
A0004650molecular_functionpolygalacturonase activity
A0005576cellular_componentextracellular region
A0005975biological_processcarbohydrate metabolic process
A0016798molecular_functionhydrolase activity, acting on glycosyl bonds
A0045490biological_processpectin catabolic process
A0071555biological_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 Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:11518536
ChainResidueDetails
AASP180

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:11518536
ChainResidueDetails
AHIS202

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: O-linked (Man...) threonine => ECO:0000269|PubMed:11518536, ECO:0007744|PDB:1IA5, ECO:0007744|PDB:1IB4
ChainResidueDetails
ATHR5
ATHR24

site_idSWS_FT_FI4
Number of Residues8
DetailsCARBOHYD: O-linked (Man...) serine => ECO:0000269|PubMed:11518536, ECO:0007744|PDB:1IA5, ECO:0007744|PDB:1IB4
ChainResidueDetails
ASER7
ASER9
ASER13
ASER14
ASER16
ASER18
ASER23
ASER34

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:11518536, ECO:0007744|PDB:1IA5, ECO:0007744|PDB:1IB4
ChainResidueDetails
AASN219

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

227561

PDB entries from 2024-11-20

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