4O0F
Crystal structure of the human L-asparaginase protein T219A mutant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001917 | cellular_component | photoreceptor inner segment |
| A | 0003948 | molecular_function | N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity |
| A | 0004067 | molecular_function | asparaginase activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008798 | molecular_function | beta-aspartyl-peptidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0033345 | biological_process | L-asparagine catabolic process via L-aspartate |
| B | 0001917 | cellular_component | photoreceptor inner segment |
| B | 0003948 | molecular_function | N4-(beta-N-acetylglucosaminyl)-L-asparaginase activity |
| B | 0004067 | molecular_function | asparaginase activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006508 | biological_process | proteolysis |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0008798 | molecular_function | beta-aspartyl-peptidase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0033345 | biological_process | L-asparagine catabolic process via L-aspartate |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 401 |
| Chain | Residue |
| A | LEU55 |
| A | GLU56 |
| A | ASP58 |
| A | PHE61 |
| A | ALA63 |
| A | CYS65 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 402 |
| Chain | Residue |
| A | THR168 |
| A | GLY220 |
| A | HOH571 |
| A | GLY11 |
| A | LEU166 |
| A | GLY167 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GLY A 403 |
| Chain | Residue |
| A | THR168 |
| A | GLY188 |
| A | ARG196 |
| A | ASP199 |
| A | SER200 |
| A | GLY220 |
| A | GLY222 |
| A | HOH559 |
| A | HOH571 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GLY A 404 |
| Chain | Residue |
| A | SER88 |
| A | ALA89 |
| A | MET109 |
| A | THR112 |
| A | HIS114 |
| A | CYS115 |
| B | LYS227 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA B 401 |
| Chain | Residue |
| B | LEU55 |
| B | GLU56 |
| B | ASP58 |
| B | PHE61 |
| B | ALA63 |
| B | CYS65 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA B 402 |
| Chain | Residue |
| B | GLY10 |
| B | GLY11 |
| B | GLY167 |
| B | THR168 |
| B | GLY220 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GLY B 403 |
| Chain | Residue |
| A | LYS227 |
| B | SER88 |
| B | ALA89 |
| B | VAL108 |
| B | MET109 |
| B | THR112 |
| B | HIS114 |
| B | CYS115 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GLY B 404 |
| Chain | Residue |
| B | THR168 |
| B | ILE189 |
| B | ARG196 |
| B | ASP199 |
| B | GLY220 |
| B | GLY222 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"19839645","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22861376","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
