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2D1I

Structure of human Atg4b

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
B0000045biological_processautophagosome assembly
B0000421cellular_componentautophagosome membrane
B0000423biological_processmitophagy
B0004175molecular_functionendopeptidase activity
B0004197molecular_functioncysteine-type endopeptidase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005776cellular_componentautophagosome
B0005783cellular_componentendoplasmic reticulum
B0005829cellular_componentcytosol
B0006508biological_processproteolysis
B0006914biological_processautophagy
B0008233molecular_functionpeptidase activity
B0008234molecular_functioncysteine-type peptidase activity
B0015031biological_processprotein transport
B0016236biological_processmacroautophagy
B0016237biological_processmicroautophagy
B0016485biological_processprotein processing
B0016787molecular_functionhydrolase activity
B0019786molecular_functionprotein-phosphatidylethanolamide deconjugating activity
B0031173biological_processotolith mineralization completed early in development
B0031410cellular_componentcytoplasmic vesicle
B0034497biological_processprotein localization to phagophore assembly site
B0034727biological_processpiecemeal microautophagy of the nucleus
B0035973biological_processaggrephagy
B0051697biological_processprotein delipidation
B0097110molecular_functionscaffold protein binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:15169837, ECO:0000269|PubMed:15187094, ECO:0000269|PubMed:16183633, ECO:0000269|PubMed:16325851, ECO:0000269|PubMed:20818167, ECO:0000269|PubMed:26378241, ECO:0000269|PubMed:28821708, ECO:0000269|PubMed:30443548
ChainResidueDetails
ACYS74
BCYS74

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000255, ECO:0000269|PubMed:16183633, ECO:0000269|PubMed:16325851
ChainResidueDetails
AASP278
BASP278

site_idSWS_FT_FI3
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:16183633, ECO:0000269|PubMed:16325851
ChainResidueDetails
AHIS280
BHIS280

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N-acetylmethionine => ECO:0000269|Ref.10, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378
ChainResidueDetails
AMET1
BMET1

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKB/AKT1 and PKB/AKT2 => ECO:0000269|PubMed:29165041, ECO:0000269|PubMed:30443548, ECO:0000269|PubMed:33607258
ChainResidueDetails
ASER34
BSER34

site_idSWS_FT_FI6
Number of Residues6
DetailsMOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:28633005
ChainResidueDetails
ACYS189
ACYS292
ACYS301
BCYS189
BCYS292
BCYS301

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine; by ULK1 => ECO:0000269|PubMed:28821708
ChainResidueDetails
ASER316
BSER316

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphoserine; by STK26 => ECO:0000269|PubMed:26378241, ECO:0000269|PubMed:29232556, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER383
BSER383

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:26378241
ChainResidueDetails
ASER392
BSER392

237735

PDB entries from 2025-06-18

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