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1X8Z

Crystal structure of a pectin methylesterase inhibitor from Arabidopsis thaliana

Functional Information from GO Data
ChainGOidnamespacecontents
A0004857molecular_functionenzyme inhibitor activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0009860biological_processpollen tube growth
A0043086biological_processnegative regulation of catalytic activity
A0046910molecular_functionpectinesterase inhibitor activity
A0048046cellular_componentapoplast
A0090404cellular_componentpollen tube tip
B0004857molecular_functionenzyme inhibitor activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0009860biological_processpollen tube growth
B0043086biological_processnegative regulation of catalytic activity
B0046910molecular_functionpectinesterase inhibitor activity
B0048046cellular_componentapoplast
B0090404cellular_componentpollen tube tip
C0004857molecular_functionenzyme inhibitor activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0009860biological_processpollen tube growth
C0043086biological_processnegative regulation of catalytic activity
C0046910molecular_functionpectinesterase inhibitor activity
C0048046cellular_componentapoplast
C0090404cellular_componentpollen tube tip
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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