5SYN
Cocrystal structure of the human acyl protein thioesterase 2 with an isoform-selective inhibitor, ML349
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004622 | molecular_function | phosphatidylcholine lysophospholipase A1 activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005795 | cellular_component | Golgi stack |
| A | 0005829 | cellular_component | cytosol |
| A | 0007411 | biological_process | axon guidance |
| A | 0008474 | molecular_function | palmitoyl-(protein) hydrolase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0045296 | molecular_function | cadherin binding |
| A | 0046464 | biological_process | acylglycerol catabolic process |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0098734 | biological_process | macromolecule depalmitoylation |
| A | 1905344 | biological_process | prostaglandin catabolic process |
| B | 0004622 | molecular_function | phosphatidylcholine lysophospholipase A1 activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005795 | cellular_component | Golgi stack |
| B | 0005829 | cellular_component | cytosol |
| B | 0007411 | biological_process | axon guidance |
| B | 0008474 | molecular_function | palmitoyl-(protein) hydrolase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0045296 | molecular_function | cadherin binding |
| B | 0046464 | biological_process | acylglycerol catabolic process |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0098734 | biological_process | macromolecule depalmitoylation |
| B | 1905344 | biological_process | prostaglandin catabolic process |
| C | 0004622 | molecular_function | phosphatidylcholine lysophospholipase A1 activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005795 | cellular_component | Golgi stack |
| C | 0005829 | cellular_component | cytosol |
| C | 0007411 | biological_process | axon guidance |
| C | 0008474 | molecular_function | palmitoyl-(protein) hydrolase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0045296 | molecular_function | cadherin binding |
| C | 0046464 | biological_process | acylglycerol catabolic process |
| C | 0070062 | cellular_component | extracellular exosome |
| C | 0098734 | biological_process | macromolecule depalmitoylation |
| C | 1905344 | biological_process | prostaglandin catabolic process |
| D | 0004622 | molecular_function | phosphatidylcholine lysophospholipase A1 activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005795 | cellular_component | Golgi stack |
| D | 0005829 | cellular_component | cytosol |
| D | 0007411 | biological_process | axon guidance |
| D | 0008474 | molecular_function | palmitoyl-(protein) hydrolase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0045296 | molecular_function | cadherin binding |
| D | 0046464 | biological_process | acylglycerol catabolic process |
| D | 0070062 | cellular_component | extracellular exosome |
| D | 0098734 | biological_process | macromolecule depalmitoylation |
| D | 1905344 | biological_process | prostaglandin catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue 71T A 301 |
| Chain | Residue |
| A | LEU33 |
| A | MET178 |
| A | VAL179 |
| A | PHE183 |
| A | LEU186 |
| A | THR187 |
| A | HIS210 |
| A | HOH429 |
| A | HOH431 |
| A | HOH452 |
| A | GLY80 |
| A | LEU81 |
| A | SER82 |
| A | PRO83 |
| A | SER122 |
| A | TRP148 |
| A | LEU149 |
| A | HIS152 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 302 |
| Chain | Residue |
| A | GLY110 |
| A | HOH469 |
| B | THR24 |
| B | PRO112 |
| B | ARG115 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | binding site for residue 71T B 301 |
| Chain | Residue |
| B | LEU33 |
| B | LEU66 |
| B | LEU78 |
| B | GLY80 |
| B | LEU81 |
| B | SER82 |
| B | PRO83 |
| B | GLU87 |
| B | SER122 |
| B | TRP148 |
| B | LEU149 |
| B | HIS152 |
| B | MET178 |
| B | VAL179 |
| B | PHE183 |
| B | LEU186 |
| B | THR187 |
| B | HIS210 |
| B | HOH416 |
| B | HOH434 |
| B | HOH443 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 302 |
| Chain | Residue |
| B | TRP75 |
| B | ASN98 |
| B | ILE99 |
| B | HOH402 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 303 |
| Chain | Residue |
| A | MET68 |
| B | SER39 |
| B | TRP40 |
| B | ALA43 |
| B | SER212 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 304 |
| Chain | Residue |
| A | GLY19 |
| B | GLU104 |
| B | HIS105 |
| B | LYS108 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 305 |
| Chain | Residue |
| A | SER39 |
| A | TRP40 |
| A | ALA43 |
| A | SER212 |
| B | MET68 |
| site_id | AC8 |
| Number of Residues | 19 |
| Details | binding site for residue 71T C 301 |
| Chain | Residue |
| C | LEU66 |
| C | GLY80 |
| C | LEU81 |
| C | SER82 |
| C | PRO83 |
| C | GLU87 |
| C | SER122 |
| C | TRP148 |
| C | LEU149 |
| C | HIS152 |
| C | MET178 |
| C | VAL179 |
| C | PHE183 |
| C | LEU186 |
| C | THR187 |
| C | HIS210 |
| C | HOH406 |
| C | HOH414 |
| C | HOH420 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue EDO C 302 |
| Chain | Residue |
| C | SER39 |
| C | TRP40 |
| C | SER212 |
| C | HOH410 |
| D | MET68 |
| site_id | AD1 |
| Number of Residues | 19 |
| Details | binding site for residue 71T D 301 |
| Chain | Residue |
| D | LEU186 |
| D | THR187 |
| D | HIS210 |
| D | HOH412 |
| D | HOH413 |
| D | HOH420 |
| D | LEU33 |
| D | LEU78 |
| D | GLY80 |
| D | LEU81 |
| D | SER82 |
| D | PRO83 |
| D | SER122 |
| D | TRP148 |
| D | LEU149 |
| D | HIS152 |
| D | MET178 |
| D | VAL179 |
| D | PHE183 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"PubMed","id":"28826475","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Charge relay system","evidences":[{"source":"UniProtKB","id":"O75608","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9QYL8","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
