2HIM
Crystal Structure and Allosteric Regulation of the Cytoplasmic Escherichia coli L-Asparaginase I
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | asparagine catabolic process via L-aspartate |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0051289 | biological_process | protein homotetramerization |
| 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 | asparagine catabolic process via L-aspartate |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0051289 | biological_process | protein homotetramerization |
| 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 | asparagine catabolic process via L-aspartate |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0051289 | biological_process | protein homotetramerization |
| 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 | 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 | 8 |
| Details | BINDING SITE FOR RESIDUE ASP A 7001 |
| Chain | Residue |
| A | GLY13 |
| A | THR14 |
| A | ASP59 |
| A | SER60 |
| A | GLY90 |
| A | THR91 |
| A | ASP92 |
| A | SER117 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ASP B 7002 |
| Chain | Residue |
| B | THR14 |
| B | ASP59 |
| B | SER60 |
| B | GLY90 |
| B | THR91 |
| B | ASP92 |
| B | SER117 |
| B | GLY13 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ASP C 7003 |
| Chain | Residue |
| A | ASN246 |
| C | GLY13 |
| C | THR14 |
| C | ASP59 |
| C | SER60 |
| C | GLY90 |
| C | THR91 |
| C | ASP92 |
| C | SER117 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ASP D 7004 |
| Chain | Residue |
| D | GLY13 |
| D | THR14 |
| D | ASP59 |
| D | SER60 |
| D | GLY90 |
| D | THR91 |
| D | ASP92 |
| D | SER117 |
| D | HOH5032 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ASN A 8001 |
| Chain | Residue |
| A | ALA162 |
| A | ARG240 |
| A | THR271 |
| A | GLN272 |
| A | CYS273 |
| A | THR301 |
| A | VAL302 |
| A | GLU303 |
| A | HOH5249 |
| A | EDO9002 |
| C | ARG240 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ASN B 8002 |
| Chain | Residue |
| B | ALA162 |
| B | ARG240 |
| B | THR271 |
| B | GLN272 |
| B | CYS273 |
| B | THR301 |
| B | VAL302 |
| B | GLU303 |
| B | HOH5398 |
| B | EDO9004 |
| D | ARG240 |
| D | HOH5101 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ASN C 8003 |
| Chain | Residue |
| A | ARG240 |
| C | ALA162 |
| C | ARG240 |
| C | THR271 |
| C | GLN272 |
| C | CYS273 |
| C | MET274 |
| C | THR301 |
| C | VAL302 |
| C | GLU303 |
| C | HOH5220 |
| C | EDO9001 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ASN D 8004 |
| Chain | Residue |
| B | ARG240 |
| D | ALA162 |
| D | ARG240 |
| D | THR271 |
| D | GLN272 |
| D | CYS273 |
| D | THR301 |
| D | VAL302 |
| D | GLU303 |
| D | HOH5151 |
| D | HOH5389 |
| D | EDO9003 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ASN A 6001 |
| Chain | Residue |
| A | GLY13 |
| A | THR14 |
| A | ASP59 |
| A | SER60 |
| A | SER61 |
| A | GLY90 |
| A | THR91 |
| A | ASP92 |
| C | ASN246 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ASN B 6002 |
| Chain | Residue |
| D | ASN246 |
| B | GLY13 |
| B | THR14 |
| B | MET17 |
| B | ASP59 |
| B | SER60 |
| B | SER61 |
| B | GLY90 |
| B | THR91 |
| B | ASP92 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ASN C 6003 |
| Chain | Residue |
| A | ASN246 |
| C | GLY13 |
| C | THR14 |
| C | MET17 |
| C | ASP59 |
| C | SER60 |
| C | SER61 |
| C | GLY90 |
| C | THR91 |
| C | ASP92 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ASN D 6004 |
| Chain | Residue |
| B | ASN246 |
| D | GLY13 |
| D | THR14 |
| D | ASP59 |
| D | SER60 |
| D | SER61 |
| D | GLY90 |
| D | THR91 |
| D | ASP92 |
| site_id | BC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EDO C 9001 |
| Chain | Residue |
| C | ASN176 |
| C | THR271 |
| C | CYS273 |
| C | MET274 |
| C | SER275 |
| C | GLY276 |
| C | ASP299 |
| C | MET300 |
| C | THR301 |
| C | ASN8003 |
| site_id | BC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EDO A 9002 |
| Chain | Residue |
| A | ASN176 |
| A | THR271 |
| A | CYS273 |
| A | MET274 |
| A | SER275 |
| A | GLY276 |
| A | ASP299 |
| A | MET300 |
| A | THR301 |
| A | ASN8001 |
| site_id | BC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO D 9003 |
| Chain | Residue |
| D | ASN176 |
| D | THR271 |
| D | CYS273 |
| D | MET274 |
| D | SER275 |
| D | GLY276 |
| D | ASP299 |
| D | MET300 |
| D | ASN8004 |
| site_id | BC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EDO B 9004 |
| Chain | Residue |
| B | ASN176 |
| B | THR271 |
| B | CYS273 |
| B | MET274 |
| B | SER275 |
| B | GLY276 |
| B | ASP299 |
| B | MET300 |
| B | THR301 |
| B | ASN8002 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 9005 |
| Chain | Residue |
| A | ASP92 |
| A | LYS163 |
| A | ALA166 |
| C | GLY243 |
| C | VAL244 |
| C | ASN246 |
| site_id | BC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 9006 |
| Chain | Residue |
| A | ILE185 |
| B | ASP92 |
| B | GLN118 |
| B | LYS163 |
| B | ALA166 |
| D | GLY243 |
| D | VAL244 |
| D | ASN246 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO C 9007 |
| Chain | Residue |
| A | GLY243 |
| A | VAL244 |
| A | ASN246 |
| C | ASP92 |
| C | LYS163 |
| C | ALA166 |
| site_id | CC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO D 9008 |
| Chain | Residue |
| B | GLY243 |
| B | VAL244 |
| B | ASN246 |
| C | ILE185 |
| D | ASP92 |
| D | GLN118 |
| D | LYS163 |
| D | ALA166 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: O-isoaspartyl threonine intermediate => ECO:0000255|PROSITE-ProRule:PRU10099, ECO:0000255|PROSITE-ProRule:PRU10100, ECO:0000269|PubMed:17451745 |
| Chain | Residue | Details |
| A | THR14 | |
| B | THR14 | |
| C | THR14 | |
| D | THR14 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0007744|PDB:2P2N |
| Chain | Residue | Details |
| B | ARG240 | |
| B | THR271 | |
| C | ASP59 | |
| C | THR91 | |
| C | ALA162 | |
| C | ARG240 | |
| C | THR271 | |
| D | ASP59 | |
| D | THR91 | |
| D | ALA162 | |
| D | ARG240 | |
| D | THR271 | |
| A | ASP59 | |
| A | THR91 | |
| A | ALA162 | |
| A | ARG240 | |
| A | THR271 | |
| B | ASP59 | |
| B | THR91 | |
| B | ALA162 |
