2O53
Crystal structure of apo-Aspartoacylase from human brain
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 | 0022010 | biological_process | central nervous system myelination |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0048714 | biological_process | positive regulation of oligodendrocyte differentiation |
| 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 | 0022010 | biological_process | central nervous system myelination |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0048714 | biological_process | positive regulation of oligodendrocyte differentiation |
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 | HIS116 |
| A | PO4315 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 A 315 |
| Chain | Residue |
| A | GLU178 |
| A | TYR288 |
| A | ZN314 |
| A | PO4316 |
| A | HOH319 |
| A | HIS21 |
| A | GLU24 |
| A | ARG63 |
| A | HIS116 |
| A | ASN117 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 316 |
| Chain | Residue |
| A | HIS21 |
| A | ARG63 |
| A | ASP68 |
| A | ASN70 |
| A | TYR288 |
| A | PO4315 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 314 |
| Chain | Residue |
| B | HIS21 |
| B | GLU24 |
| B | HIS116 |
| B | PO4315 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 B 315 |
| Chain | Residue |
| B | HIS21 |
| B | GLU24 |
| B | ARG63 |
| B | HIS116 |
| B | ASN117 |
| B | GLU178 |
| B | TYR288 |
| B | ZN314 |
| B | PO4316 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 B 316 |
| Chain | Residue |
| B | HIS21 |
| B | ARG63 |
| B | ASP68 |
| B | ASN70 |
| B | TYR164 |
| B | TYR288 |
| B | PO4315 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor/acceptor => ECO:0000305|PubMed:17027983, ECO:0000305|PubMed:18293939, ECO:0007744|PDB:2O4H |
| Chain | Residue | Details |
| A | GLU178 | |
| B | GLU178 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17027983, ECO:0000269|PubMed:18293939, ECO:0007744|PDB:2O4H, ECO:0007744|PDB:2O53 |
| Chain | Residue | Details |
| A | HIS21 | |
| A | GLU24 | |
| A | HIS116 | |
| B | HIS21 | |
| B | GLU24 | |
| B | HIS116 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18293939, ECO:0007744|PDB:2O4H |
| Chain | Residue | Details |
| A | ARG63 | |
| B | TYR288 | |
| A | ASN70 | |
| A | TYR164 | |
| A | ARG168 | |
| A | TYR288 | |
| B | ARG63 | |
| B | ASN70 | |
| B | TYR164 | |
| B | ARG168 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18293939, ECO:0007744|PDB:2O4H, ECO:0007744|PDB:2O53 |
| Chain | Residue | Details |
| A | ARG71 | |
| B | ARG71 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Transition state stabilizer => ECO:0000305|PubMed:17027983, ECO:0000305|PubMed:18293939, ECO:0007744|PDB:2O4H |
| Chain | Residue | Details |
| A | ARG63 | |
| B | ARG63 |
