2Z0E
The crystal structure of human Atg4B- LC3(1-124) complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000045 | biological_process | autophagosome assembly |
| A | 0000421 | cellular_component | autophagosome membrane |
| A | 0000423 | biological_process | mitophagy |
| A | 0004175 | molecular_function | endopeptidase activity |
| A | 0004197 | molecular_function | cysteine-type endopeptidase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005776 | cellular_component | autophagosome |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005829 | cellular_component | cytosol |
| A | 0006508 | biological_process | proteolysis |
| A | 0006914 | biological_process | autophagy |
| A | 0008234 | molecular_function | cysteine-type peptidase activity |
| A | 0015031 | biological_process | protein transport |
| A | 0016236 | biological_process | macroautophagy |
| A | 0016237 | biological_process | microautophagy |
| A | 0016485 | biological_process | protein processing |
| A | 0019786 | molecular_function | protein-phosphatidylethanolamide deconjugating activity |
| A | 0031173 | biological_process | otolith mineralization completed early in development |
| A | 0031410 | cellular_component | cytoplasmic vesicle |
| A | 0034497 | biological_process | protein localization to phagophore assembly site |
| A | 0034727 | biological_process | piecemeal microautophagy of the nucleus |
| A | 0035973 | biological_process | aggrephagy |
| A | 0051697 | biological_process | protein delipidation |
| A | 0097110 | molecular_function | scaffold protein binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | SITE: Cleavage; by ATG4B => ECO:0000269|PubMed:11060023, ECO:0000269|PubMed:16183633 |
| Chain | Residue | Details |
| B | GLY120 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | LIPID: Phosphatidylserine amidated glycine; alternate => ECO:0000250|UniProtKB:Q9GZQ8 |
| Chain | Residue | Details |
| B | GLY120 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | ACT_SITE: ACT_SITE => ECO:0000269|PubMed:16183633, ECO:0000269|PubMed:16325851 |
| Chain | Residue | Details |
| A | ALA280 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylmethionine => ECO:0000269|Ref.10, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378 |
| Chain | Residue | Details |
| A | MET1 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PKB/AKT1 and PKB/AKT2 => ECO:0000269|PubMed:29165041, ECO:0000269|PubMed:30443548, ECO:0000269|PubMed:33607258 |
| Chain | Residue | Details |
| A | SER34 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 3 |
| Details | MOD_RES: S-nitrosocysteine => ECO:0000269|PubMed:28633005 |
| Chain | Residue | Details |
| A | CYS189 | |
| A | CYS292 | |
| A | CYS301 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by ULK1 => ECO:0000269|PubMed:28821708 |
| Chain | Residue | Details |
| A | SER316 |
