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3WOG

Crystal structure plant lectin in complex with ligand

Functional Information from GO Data
ChainGOidnamespacecontents
A0005537molecular_functionD-mannose binding
A0006952biological_processdefense response
A0030246molecular_functioncarbohydrate binding
A0035821biological_processmodulation of process of another organism
A0090729molecular_functiontoxin activity
B0005537molecular_functionD-mannose binding
B0006952biological_processdefense response
B0030246molecular_functioncarbohydrate binding
B0035821biological_processmodulation of process of another organism
B0090729molecular_functiontoxin activity
Functional Information from PROSITE/UniProt
site_idPS00307
Number of Residues7
DetailsLECTIN_LEGUME_BETA Legume lectins beta-chain signature. VAVEFDT
ChainResidueDetails
AVAL142-THR148

site_idPS00308
Number of Residues10
DetailsLECTIN_LEGUME_ALPHA Legume lectins alpha-chain signature. LPEWVIVGFT
ChainResidueDetails
ALEU222-THR231

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:3089787, ECO:0000269|Ref.2
ChainResidueDetails
AASN33
BASN33

site_idSWS_FT_FI2
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:3089787, ECO:0000269|Ref.2
ChainResidueDetails
AASN81
BASN81

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine
ChainResidueDetails
AASN101
BASN101

226707

PDB entries from 2024-10-30

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