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2Z0D

The crystal structure of human Atg4B- LC3(1-120) complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0000045biological_processautophagosome assembly
A0000421cellular_componentautophagosome membrane
A0000423biological_processmitophagy
A0004175molecular_functionendopeptidase activity
A0004197molecular_functioncysteine-type endopeptidase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005776cellular_componentautophagosome
A0005783cellular_componentendoplasmic reticulum
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0006914biological_processautophagy
A0008233molecular_functionpeptidase activity
A0008234molecular_functioncysteine-type peptidase activity
A0015031biological_processprotein transport
A0016236biological_processmacroautophagy
A0016237biological_processmicroautophagy
A0016485biological_processprotein processing
A0016787molecular_functionhydrolase activity
A0019786molecular_functionprotein-phosphatidylethanolamide deconjugating activity
A0031173biological_processotolith mineralization completed early in development
A0031410cellular_componentcytoplasmic vesicle
A0034497biological_processprotein localization to phagophore assembly site
A0034727biological_processpiecemeal microautophagy of the nucleus
A0035973biological_processaggrephagy
A0051697biological_processprotein delipidation
A0097110molecular_functionscaffold protein binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"15169837","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15187094","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16183633","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16325851","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20818167","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26378241","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"28821708","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30443548","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16183633","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16325851","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"16183633","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16325851","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PKB/AKT1 and PKB/AKT2","evidences":[{"source":"PubMed","id":"29165041","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30443548","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"33607258","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"28633005","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by ULK1","evidences":[{"source":"PubMed","id":"28821708","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsLipidation: {"description":"Phosphatidylserine amidated glycine; alternate","evidences":[{"source":"UniProtKB","id":"Q9GZQ8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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PDB entries from 2025-07-30

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