1JSL
Crystal structure of Erwinia chrysanthemi L-asparaginase complexed with 6-HYDROXY-D-NORLEUCINE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004067 | molecular_function | asparaginase activity |
| A | 0006520 | biological_process | amino acid metabolic process |
| A | 0006528 | biological_process | asparagine metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| B | 0004067 | molecular_function | asparaginase activity |
| B | 0006520 | biological_process | amino acid metabolic process |
| B | 0006528 | biological_process | asparagine metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| C | 0004067 | molecular_function | asparaginase activity |
| C | 0006520 | biological_process | amino acid metabolic process |
| C | 0006528 | biological_process | asparagine metabolic process |
| C | 0016787 | molecular_function | hydrolase activity |
| D | 0004067 | molecular_function | asparaginase activity |
| D | 0006520 | biological_process | amino acid metabolic process |
| D | 0006528 | biological_process | asparagine metabolic process |
| D | 0016787 | molecular_function | hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE DDO A 2401 |
| Chain | Residue |
| A | GLY14 |
| A | ALA120 |
| A | MET121 |
| A | HOH2502 |
| A | HOH2506 |
| A | HOH2508 |
| A | HOH2510 |
| A | THR15 |
| A | TYR29 |
| A | ALA61 |
| A | SER62 |
| A | GLU63 |
| A | GLY94 |
| A | THR95 |
| A | ASP96 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE DDO B 2402 |
| Chain | Residue |
| B | GLY14 |
| B | THR15 |
| B | TYR29 |
| B | ALA61 |
| B | SER62 |
| B | GLU63 |
| B | GLY94 |
| B | THR95 |
| B | ASP96 |
| B | ALA120 |
| B | MET121 |
| B | HOH2403 |
| B | HOH2408 |
| D | HOH2604 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE DDO C 2403 |
| Chain | Residue |
| A | SER254 |
| A | HOH2740 |
| C | GLY14 |
| C | THR15 |
| C | TYR29 |
| C | ALA61 |
| C | SER62 |
| C | GLU63 |
| C | GLY94 |
| C | THR95 |
| C | ASP96 |
| C | ALA120 |
| C | MET121 |
| C | HOH2605 |
| C | HOH2609 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE DDO D 2404 |
| Chain | Residue |
| B | SER254 |
| B | HOH2635 |
| D | GLY14 |
| D | THR15 |
| D | TYR29 |
| D | ALA61 |
| D | SER62 |
| D | GLU63 |
| D | GLY94 |
| D | THR95 |
| D | ASP96 |
| D | ALA120 |
| D | MET121 |
| D | HOH2609 |
| D | HOH2613 |
| D | HOH2615 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 1PE A 2501 |
| Chain | Residue |
| A | GLY241 |
| A | LYS243 |
| A | HOH2628 |
| A | HOH2690 |
| C | ASP210 |
| C | ARG212 |
| C | THR312 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL C 2601 |
| Chain | Residue |
| A | ASP68 |
| A | SER216 |
| A | LEU217 |
| A | LYS219 |
| A | MET308 |
| A | HOH2574 |
| C | THR215 |
| C | HOH2604 |
| C | HOH2624 |
| site_id | AC7 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL D 2602 |
| Chain | Residue |
| B | LEU267 |
| B | PRO291 |
| B | GLY292 |
| B | PRO317 |
| B | HOH2444 |
| B | HOH2637 |
| D | ARG313 |
| D | THR314 |
| D | SER315 |
| D | ASP316 |
| D | HOH2607 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL C 2603 |
| Chain | Residue |
| C | ALA82 |
| C | ARG83 |
| C | ASP84 |
| C | ASP85 |
Functional Information from PROSITE/UniProt
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1288 |
| Details | Domain: {"description":"Asparaginase/glutaminase","evidences":[{"source":"PROSITE-ProRule","id":"PRU01068","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| 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":"11755201","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8348975","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| 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 | THR15 | |
| A | THR95 | |
| A | ASP96 | |
| A | TYR29 | |
| A | LYS168 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| B | THR15 | |
| B | THR95 | |
| B | ASP96 | |
| B | TYR29 | |
| B | LYS168 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| C | THR15 | |
| C | THR95 | |
| C | ASP96 | |
| C | TYR29 | |
| C | LYS168 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| D | THR15 | |
| D | THR95 | |
| D | ASP96 | |
| D | TYR29 | |
| D | LYS168 |
| site_id | CSA5 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| A | VAL284 | |
| C | THR15 | |
| C | THR95 | |
| C | TYR29 |
| site_id | CSA6 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| D | THR15 | |
| D | THR95 | |
| D | TYR29 | |
| B | VAL284 |
| site_id | CSA7 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| A | THR15 | |
| A | THR95 | |
| A | TYR29 | |
| C | VAL284 |
| site_id | CSA8 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 3eca |
| Chain | Residue | Details |
| D | VAL284 | |
| B | THR15 | |
| B | THR95 | |
| B | TYR29 |
