6WQZ
Structure of human ATG9A, the only transmembrane protein of the core autophagy machinery
Functional Information from GO Data
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | binding site for residue LMN C 801 |
Chain | Residue |
C | ILE135 |
C | ARG245 |
C | TYR249 |
C | ASN297 |
C | LEU300 |
C | ILE304 |
C | TRP307 |
C | TYR311 |
C | LMN802 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue LMN C 802 |
Chain | Residue |
C | LEU45 |
C | TYR249 |
C | TRP257 |
C | LMN801 |
site_id | AC3 |
Number of Residues | 9 |
Details | binding site for residue LMN B 801 |
Chain | Residue |
B | ILE135 |
B | ARG245 |
B | TYR249 |
B | ASN297 |
B | LEU300 |
B | ILE304 |
B | TRP307 |
B | TYR311 |
B | LMN802 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue LMN B 802 |
Chain | Residue |
B | LEU45 |
B | TYR249 |
B | TRP257 |
B | LMN801 |
site_id | AC5 |
Number of Residues | 9 |
Details | binding site for residue LMN A 801 |
Chain | Residue |
A | ILE135 |
A | ARG245 |
A | TYR249 |
A | ASN297 |
A | LEU300 |
A | ILE304 |
A | TRP307 |
A | TYR311 |
A | LMN802 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue LMN A 802 |
Chain | Residue |
A | LEU45 |
A | TYR249 |
A | TRP257 |
A | LMN801 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1800 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000305 |
Chain | Residue | Details |
C | ALA2-CYS61 | |
F | ALA329-PRO371 | |
F | ILE425-GLN470 | |
F | LEU481-PRO483 | |
B | ALA2-CYS61 | |
B | CYS155-ILE290 | |
B | PRO302-VAL319 | |
B | ALA329-PRO371 | |
B | ILE425-GLN470 | |
B | LEU481-PRO483 | |
A | ALA2-CYS61 | |
C | CYS155-ILE290 | |
A | CYS155-ILE290 | |
A | PRO302-VAL319 | |
A | ALA329-PRO371 | |
A | ILE425-GLN470 | |
A | LEU481-PRO483 | |
E | ALA2-CYS61 | |
E | CYS155-ILE290 | |
E | PRO302-VAL319 | |
E | ALA329-PRO371 | |
E | ILE425-GLN470 | |
C | PRO302-VAL319 | |
E | LEU481-PRO483 | |
D | ALA2-CYS61 | |
D | CYS155-ILE290 | |
D | PRO302-VAL319 | |
D | ALA329-PRO371 | |
D | ILE425-GLN470 | |
D | LEU481-PRO483 | |
C | ALA329-PRO371 | |
C | ILE425-GLN470 | |
C | LEU481-PRO483 | |
F | ALA2-CYS61 | |
F | CYS155-ILE290 | |
F | PRO302-VAL319 |
site_id | SWS_FT_FI2 |
Number of Residues | 534 |
Details | TRANSMEM: Helical => ECO:0000269|PubMed:32610138, ECO:0000269|PubMed:33106659, ECO:0007744|PDB:6WQZ, ECO:0007744|PDB:6WR4, ECO:0007744|PDB:7JLO, ECO:0007744|PDB:7JLP, ECO:0007744|PDB:7JLQ |
Chain | Residue | Details |
C | MET62-VAL84 | |
B | ASN129-ILE154 | |
B | LEU372-TYR397 | |
B | VAL407-PHE424 | |
A | MET62-VAL84 | |
A | ASN129-ILE154 | |
A | LEU372-TYR397 | |
A | VAL407-PHE424 | |
E | MET62-VAL84 | |
E | ASN129-ILE154 | |
E | LEU372-TYR397 | |
C | ASN129-ILE154 | |
E | VAL407-PHE424 | |
D | MET62-VAL84 | |
D | ASN129-ILE154 | |
D | LEU372-TYR397 | |
D | VAL407-PHE424 | |
C | LEU372-TYR397 | |
C | VAL407-PHE424 | |
F | MET62-VAL84 | |
F | ASN129-ILE154 | |
F | LEU372-TYR397 | |
F | VAL407-PHE424 | |
B | MET62-VAL84 |
site_id | SWS_FT_FI3 |
Number of Residues | 306 |
Details | TOPO_DOM: Lumenal => ECO:0000305 |
Chain | Residue | Details |
C | SER85-GLU128 | |
E | ASP398-HIS406 | |
D | SER85-GLU128 | |
D | ASP398-HIS406 | |
C | ASP398-HIS406 | |
F | SER85-GLU128 | |
F | ASP398-HIS406 | |
B | SER85-GLU128 | |
B | ASP398-HIS406 | |
A | SER85-GLU128 | |
A | ASP398-HIS406 | |
E | SER85-GLU128 |
site_id | SWS_FT_FI4 |
Number of Residues | 60 |
Details | INTRAMEM: INTRAMEM => ECO:0000269|PubMed:32610138, ECO:0000269|PubMed:33106659, ECO:0007744|PDB:6WQZ, ECO:0007744|PDB:6WR4, ECO:0007744|PDB:7JLP, ECO:0007744|PDB:7JLQ |
Chain | Residue | Details |
C | LEU291-CYS301 | |
F | LEU291-CYS301 | |
B | LEU291-CYS301 | |
A | LEU291-CYS301 | |
E | LEU291-CYS301 | |
D | LEU291-CYS301 |
site_id | SWS_FT_FI5 |
Number of Residues | 48 |
Details | INTRAMEM: INTRAMEM => ECO:0000269|PubMed:32610138, ECO:0000269|PubMed:33106659, ECO:0007744|PDB:6WQZ, ECO:0007744|PDB:6WR4, ECO:0007744|PDB:7JLO, ECO:0007744|PDB:7JLP, ECO:0007744|PDB:7JLQ |
Chain | Residue | Details |
C | LEU320-GLY328 | |
F | LEU320-GLY328 | |
B | LEU320-GLY328 | |
A | LEU320-GLY328 | |
E | LEU320-GLY328 | |
D | LEU320-GLY328 |
site_id | SWS_FT_FI6 |
Number of Residues | 54 |
Details | INTRAMEM: INTRAMEM => ECO:0000269|PubMed:32610138, ECO:0007744|PDB:6WQZ |
Chain | Residue | Details |
C | TYR471-LEU480 | |
F | TYR471-LEU480 | |
B | TYR471-LEU480 | |
A | TYR471-LEU480 | |
E | TYR471-LEU480 | |
D | TYR471-LEU480 |
site_id | SWS_FT_FI7 |
Number of Residues | 48 |
Details | INTRAMEM: INTRAMEM => ECO:0000269|PubMed:32610138, ECO:0000269|PubMed:33106659, ECO:0007744|PDB:6WQZ, ECO:0007744|PDB:7JLP |
Chain | Residue | Details |
C | ILE484-PHE492 | |
F | ILE484-PHE492 | |
B | ILE484-PHE492 | |
A | ILE484-PHE492 | |
E | ILE484-PHE492 | |
D | ILE484-PHE492 |
site_id | SWS_FT_FI8 |
Number of Residues | 6 |
Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378 |
Chain | Residue | Details |
C | ALA2 | |
F | ALA2 | |
B | ALA2 | |
A | ALA2 | |
E | ALA2 | |
D | ALA2 |
site_id | SWS_FT_FI9 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
C | SER14 | |
F | SER14 | |
B | SER14 | |
A | SER14 | |
E | SER14 | |
D | SER14 |
site_id | SWS_FT_FI10 |
Number of Residues | 6 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q68FE2 |
Chain | Residue | Details |
C | SER16 | |
F | SER16 | |
B | SER16 | |
A | SER16 | |
E | SER16 | |
D | SER16 |
site_id | SWS_FT_FI11 |
Number of Residues | 12 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
C | SER18 | |
E | SER656 | |
D | SER18 | |
D | SER656 | |
C | SER656 | |
F | SER18 | |
F | SER656 | |
B | SER18 | |
B | SER656 | |
A | SER18 | |
A | SER656 | |
E | SER18 |
site_id | SWS_FT_FI12 |
Number of Residues | 6 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16940348, ECO:0000269|PubMed:27316455 |
Chain | Residue | Details |
C | ASN99 | |
F | ASN99 | |
B | ASN99 | |
A | ASN99 | |
E | ASN99 | |
D | ASN99 |