2P2D
Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia coli L-Asparaginase I
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004067 | molecular_function | asparaginase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0033345 | biological_process | L-asparagine catabolic process via L-aspartate |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0051289 | biological_process | protein homotetramerization |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004067 | molecular_function | asparaginase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0033345 | biological_process | L-asparagine catabolic process via L-aspartate |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0051289 | biological_process | protein homotetramerization |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0004067 | molecular_function | asparaginase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0033345 | biological_process | L-asparagine catabolic process via L-aspartate |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0051289 | biological_process | protein homotetramerization |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0004067 | molecular_function | asparaginase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0033345 | biological_process | L-asparagine catabolic process via L-aspartate |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 7001 |
| Chain | Residue |
| A | SER102 |
| A | LEU105 |
| A | ASN107 |
| A | LEU108 |
| A | PRO196 |
| A | ARG331 |
| A | HOH9027 |
| A | HOH9030 |
| A | HOH9098 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 7002 |
| Chain | Residue |
| C | ASN176 |
| C | THR271 |
| C | MET274 |
| C | SER275 |
| C | GLY276 |
| C | MET300 |
| C | HOH9014 |
| C | HOH9121 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 7003 |
| Chain | Residue |
| C | SER102 |
| C | LEU105 |
| C | LEU108 |
| C | PRO196 |
| C | ARG331 |
| C | HOH9038 |
| C | HOH9052 |
| C | HOH9089 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 7004 |
| Chain | Residue |
| A | ARG240 |
| A | THR271 |
| A | CYS273 |
| A | MET300 |
| A | VAL302 |
| A | HOH9017 |
| A | HOH9059 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 7005 |
| Chain | Residue |
| D | SER102 |
| D | LEU105 |
| D | ASN107 |
| D | LEU108 |
| D | PRO196 |
| D | ARG331 |
| D | HOH9031 |
| D | HOH9038 |
| D | HOH9044 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 7006 |
| Chain | Residue |
| D | ASN176 |
| D | MET274 |
| D | SER275 |
| D | GLY276 |
| D | MET300 |
| D | HOH9025 |
| D | HOH9116 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 7007 |
| Chain | Residue |
| B | SER102 |
| B | LEU105 |
| B | LEU108 |
| B | PRO196 |
| B | ARG331 |
| B | HOH9048 |
| B | HOH9052 |
| B | HOH9068 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 7008 |
| Chain | Residue |
| B | ASN176 |
| B | THR271 |
| B | MET274 |
| B | SER275 |
| B | GLY276 |
| B | MET300 |
| B | HOH9029 |
| B | HOH9033 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 9001 |
| Chain | Residue |
| A | GLY13 |
| A | MET58 |
| A | SER60 |
| A | GLY90 |
| A | THR91 |
| A | ASP92 |
| A | HOH9083 |
| A | HOH9166 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 9002 |
| Chain | Residue |
| B | GLY13 |
| B | THR14 |
| B | ASP59 |
| B | SER60 |
| B | GLY90 |
| B | THR91 |
| B | ASP92 |
| B | HOH9138 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL C 9003 |
| Chain | Residue |
| C | GLY13 |
| C | THR14 |
| C | MET58 |
| C | ASP59 |
| C | SER60 |
| C | GLY90 |
| C | THR91 |
| C | ASP92 |
| C | HOH9132 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL D 9004 |
| Chain | Residue |
| D | GLY13 |
| D | MET58 |
| D | ASP59 |
| D | SER60 |
| D | GLY90 |
| D | THR91 |
| D | ASP92 |
| D | HOH9062 |
| D | HOH9134 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"O-isoaspartyl threonine intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10099","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10100","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17451745","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"2P2N","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| A | TYR24 | |
| A | ASP92 | |
| A | THR14 | |
| A | THR91 | |
| A | LYS163 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| B | TYR24 | |
| B | ASP92 | |
| B | THR14 | |
| B | THR91 | |
| B | LYS163 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| C | TYR24 | |
| C | ASP92 | |
| C | THR14 | |
| C | THR91 | |
| C | LYS163 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| D | TYR24 | |
| D | ASP92 | |
| D | THR14 | |
| D | THR91 | |
| D | LYS163 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| A | LEU289 | |
| C | TYR24 | |
| C | THR14 | |
| C | THR91 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| D | TYR24 | |
| D | THR14 | |
| D | THR91 | |
| B | LEU289 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| A | TYR24 | |
| A | THR14 | |
| A | THR91 | |
| C | LEU289 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| D | LEU289 | |
| B | TYR24 | |
| B | THR14 | |
| B | THR91 |
