2Q51
Ensemble refinement of the protein crystal structure of an aspartoacylase from Homo sapiens
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006083 | biological_process | acetate metabolic process |
| A | 0006531 | biological_process | aspartate metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| A | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| A | 0019807 | molecular_function | aspartoacylase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006083 | biological_process | acetate metabolic process |
| B | 0006531 | biological_process | aspartate metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016788 | molecular_function | hydrolase activity, acting on ester bonds |
| B | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| B | 0019807 | molecular_function | aspartoacylase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 314 |
| Chain | Residue |
| A | HIS21 |
| A | GLU24 |
| A | ARG63 |
| A | HIS116 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 315 |
| Chain | Residue |
| A | ASN70 |
| A | ILE127 |
| A | ILE157 |
| A | ARG168 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 316 |
| Chain | Residue |
| A | ARG63 |
| A | ASP68 |
| A | ASN70 |
| A | ARG71 |
| A | TYR288 |
| A | HIS21 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 317 |
| Chain | Residue |
| A | LYS103 |
| A | ASP104 |
| A | LYS163 |
| A | TYR164 |
| B | LYS163 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 A 318 |
| Chain | Residue |
| A | ARG71 |
| A | HIS159 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 314 |
| Chain | Residue |
| B | HIS21 |
| B | GLU24 |
| B | HIS116 |
| B | PO4315 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 B 315 |
| Chain | Residue |
| B | GLU24 |
| B | ARG63 |
| B | ASN117 |
| B | THR118 |
| B | GLU178 |
| B | GLU285 |
| B | ZN314 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 316 |
| Chain | Residue |
| B | HIS21 |
| B | ARG63 |
| B | ASP68 |
| B | ASN70 |
| B | ARG71 |
| B | LYS291 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 B 317 |
| Chain | Residue |
| B | LYS103 |
| B | ASP104 |
| B | LYS163 |
| B | TYR164 |
| B | SER169 |
| B | HOH338 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 B 318 |
| Chain | Residue |
| B | ARG71 |
| B | HIS159 |
| B | LYS228 |
| B | HOH329 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"17027983","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"18293939","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2O4H","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17027983","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18293939","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2O4H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O53","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18293939","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2O4H","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"18293939","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2O4H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O53","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"PubMed","id":"17027983","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"18293939","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2O4H","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
