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1CZF

ENDO-POLYGALACTURONASE II FROM ASPERGILLUS NIGER

Functional Information from GO Data
ChainGOidnamespacecontents
A0004650molecular_functionpolygalacturonase activity
A0005975biological_processcarbohydrate metabolic process
B0004650molecular_functionpolygalacturonase activity
B0005975biological_processcarbohydrate metabolic process
Functional Information from PROSITE/UniProt
site_idPS00502
Number of Residues14
DetailsPOLYGALACTURONASE Polygalacturonase active site. GgtCigGHGLs.IGS
ChainResidueDetails
AGLY216-SER229

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:10521427
ChainResidueDetails
AASP201
BASP201

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:10521427
ChainResidueDetails
AHIS223
BHIS223

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:10521427, ECO:0000269|PubMed:9276972
ChainResidueDetails
AASN240
BASN240

Catalytic Information from CSA
site_idCSA1
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 10521427, 11518536
ChainResidueDetails
AASP202
AASP180
AASP201
AHIS223

site_idMCSA1
Number of Residues6
DetailsM-CSA 480
ChainResidueDetails
AASP180proton shuttle (general acid/base)
AASP201proton shuttle (general acid/base)
AASP202electrostatic stabiliser
AHIS223proton shuttle (general acid/base)
AARG256modifies pKa
ALYS258modifies pKa

site_idMCSA2
Number of Residues6
DetailsM-CSA 480
ChainResidueDetails
BASP180proton shuttle (general acid/base)
BASP201proton shuttle (general acid/base)
BASP202electrostatic stabiliser
BHIS223proton shuttle (general acid/base)
BARG256modifies pKa
BLYS258modifies pKa

237992

PDB entries from 2025-06-25

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