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3WAN

Crystal structure of Atg13 LIR-fused human LC3A_2-121

Functional Information from GO Data
ChainGOidnamespacecontents
A0000045biological_processautophagosome assembly
A0000421cellular_componentautophagosome membrane
A0000422biological_processautophagy of mitochondrion
A0005515molecular_functionprotein binding
A0005543molecular_functionphospholipid binding
A0005737cellular_componentcytoplasm
A0005770cellular_componentlate endosome
A0005776cellular_componentautophagosome
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005874cellular_componentmicrotubule
A0006914biological_processautophagy
A0006995biological_processcellular response to nitrogen starvation
A0007254biological_processJNK cascade
A0008017molecular_functionmicrotubule binding
A0008429molecular_functionphosphatidylethanolamine binding
A0009267biological_processcellular response to starvation
A0010040biological_processresponse to iron(II) ion
A0010288biological_processresponse to lead ion
A0012505cellular_componentendomembrane system
A0016020cellular_componentmembrane
A0016236biological_processmacroautophagy
A0031090cellular_componentorganelle membrane
A0031410cellular_componentcytoplasmic vesicle
A0031625molecular_functionubiquitin protein ligase binding
A0031667biological_processresponse to nutrient levels
A0034198biological_processcellular response to amino acid starvation
A0038066biological_processp38MAPK cascade
A0043231cellular_componentintracellular membrane-bounded organelle
A0044754cellular_componentautolysosome
A0045202cellular_componentsynapse
A0060395biological_processSMAD protein signal transduction
A0070301biological_processcellular response to hydrogen peroxide
A0071280biological_processcellular response to copper ion
A0090650biological_processcellular response to oxygen-glucose deprivation
A0097352biological_processautophagosome maturation
A0098978cellular_componentglutamatergic synapse
B0000045biological_processautophagosome assembly
B0000421cellular_componentautophagosome membrane
B0000422biological_processautophagy of mitochondrion
B0005515molecular_functionprotein binding
B0005543molecular_functionphospholipid binding
B0005737cellular_componentcytoplasm
B0005770cellular_componentlate endosome
B0005776cellular_componentautophagosome
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005874cellular_componentmicrotubule
B0006914biological_processautophagy
B0006995biological_processcellular response to nitrogen starvation
B0007254biological_processJNK cascade
B0008017molecular_functionmicrotubule binding
B0008429molecular_functionphosphatidylethanolamine binding
B0009267biological_processcellular response to starvation
B0010040biological_processresponse to iron(II) ion
B0010288biological_processresponse to lead ion
B0012505cellular_componentendomembrane system
B0016020cellular_componentmembrane
B0016236biological_processmacroautophagy
B0031090cellular_componentorganelle membrane
B0031410cellular_componentcytoplasmic vesicle
B0031625molecular_functionubiquitin protein ligase binding
B0031667biological_processresponse to nutrient levels
B0034198biological_processcellular response to amino acid starvation
B0038066biological_processp38MAPK cascade
B0043231cellular_componentintracellular membrane-bounded organelle
B0044754cellular_componentautolysosome
B0045202cellular_componentsynapse
B0060395biological_processSMAD protein signal transduction
B0070301biological_processcellular response to hydrogen peroxide
B0071280biological_processcellular response to copper ion
B0090650biological_processcellular response to oxygen-glucose deprivation
B0097352biological_processautophagosome maturation
B0098978cellular_componentglutamatergic synapse
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE MPD A 201
ChainResidue
AHOH387

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsSITE: Cleavage; by ATG4B => ECO:0000305|PubMed:15187094
ChainResidueDetails
AGLY136
BGLY136

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:20713600
ChainResidueDetails
ASER28
BSER28

site_idSWS_FT_FI3
Number of Residues2
DetailsLIPID: Phosphatidylserine amidated glycine; alternate => ECO:0000269|PubMed:33909989
ChainResidueDetails
AGLY136
BGLY136

218853

PDB entries from 2024-04-24

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