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8YN1

Cryo-EM structure of NRG1A(LRR) in complex with EDS1-SAG101-(ADPr-ATP)

Functional Information from GO Data
ChainGOidnamespacecontents
A0000304biological_processresponse to singlet oxygen
A0001666biological_processresponse to hypoxia
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006629biological_processlipid metabolic process
A0006952biological_processdefense response
A0009507cellular_componentchloroplast
A0009626biological_processplant-type hypersensitive response
A0009627biological_processsystemic acquired resistance
A0009862biological_processsystemic acquired resistance, salicylic acid mediated signaling pathway
A0010310biological_processregulation of hydrogen peroxide metabolic process
A0010618biological_processaerenchyma formation
A0016298molecular_functionlipase activity
A0016787molecular_functionhydrolase activity
A0042803molecular_functionprotein homodimerization activity
A0050829biological_processdefense response to Gram-negative bacterium
A0060866biological_processleaf abscission
B0006629biological_processlipid metabolic process
B0006952biological_processdefense response
B0052689molecular_functioncarboxylic ester hydrolase activity
Functional Information from PROSITE/UniProt
site_idPS00120
Number of Residues10
DetailsLIPASE_SER Lipases, serine active site. IVFTGHSSGG
ChainResidueDetails
AILE117-GLY126

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues46
DetailsCoiled coil: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"P19515","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"UniProtKB","id":"P19515","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues20
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues22
DetailsRepeat: {"description":"LRR 1"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues22
DetailsRepeat: {"description":"LRR 2"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues22
DetailsRepeat: {"description":"LRR 3"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues22
DetailsRepeat: {"description":"LRR 4"}
ChainResidueDetails

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PDB entries from 2026-01-28

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