2ZZP
The crystal structure of human Atg4B(C74S)- 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 | ACT_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 |
Chain | Residue | Details |
A | SER74 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: ACT_SITE => ECO:0000255, ECO:0000269|PubMed:16183633, ECO:0000269|PubMed:16325851 |
Chain | Residue | Details |
A | ASP278 |
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 | HIS280 |
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 |