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1IDK

PECTIN LYASE A

Functional Information from GO Data
ChainGOidnamespacecontents
A0000272biological_processpolysaccharide catabolic process
A0005576cellular_componentextracellular region
A0016829molecular_functionlyase activity
A0030570molecular_functionpectate lyase activity
A0047490molecular_functionpectin lyase activity
A0071555biological_processcell wall organization
Functional Information from PDB Data
site_idCAT
Number of Residues3
DetailsTHIS IS THE PUTATIVE ACTIVE SITE OF THE ENZYME.
ChainResidue
AASP154
AARG176
AARG236

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000255
ChainResidueDetails
AARG236

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: O-linked (Man) threonine
ChainResidueDetails
ATHR68

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305
ChainResidueDetails
AASN109

site_idSWS_FT_FI4
Number of Residues1
DetailsCARBOHYD: O-linked (Man) serine; in strain 4M-147
ChainResidueDetails
ASER348

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1idj
ChainResidueDetails
AARG236
AARG176

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1idj
ChainResidueDetails
AARG236
AASP154

site_idMCSA1
Number of Residues4
DetailsM-CSA 590
ChainResidueDetails
AASP154electrostatic stabiliser
AARG176electrostatic stabiliser
AARG236proton shuttle (general acid/base)
ALYS239electrostatic stabiliser

225158

PDB entries from 2024-09-18

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