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3WAL

Crystal structure of human LC3A_2-121

Functional Information from GO Data
ChainGOidnamespacecontents
A0000045biological_processautophagosome assembly
A0000421cellular_componentautophagosome membrane
A0000422biological_processautophagy of mitochondrion
A0000423biological_processmitophagy
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
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MLT A 201
ChainResidue
ALYS12
ALYS12
APHE17
AARG20
AASP108
AHOH320
AHOH373

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsSITE: Cleavage; by ATG4B => ECO:0000305|PubMed:15187094
ChainResidueDetails
AGLY124

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine; by PKA => ECO:0000269|PubMed:20713600
ChainResidueDetails
ASER16

site_idSWS_FT_FI3
Number of Residues1
DetailsLIPID: Phosphatidylserine amidated glycine; alternate => ECO:0000269|PubMed:33909989
ChainResidueDetails
AGLY124

227344

PDB entries from 2024-11-13

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