4PVS
Crystal structure of fully-cleaved human l-asparaginase protein in complex with l-aspartate
Replaces: 4GDWFunctional 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 | 9 |
Details | BINDING SITE FOR RESIDUE ASP A 402 |
Chain | Residue |
A | ASP199 |
A | THR219 |
A | GLY220 |
A | GLY222 |
A | HOH503 |
A | HOH569 |
A | THR168 |
A | GLY188 |
A | ARG196 |
site_id | AC3 |
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 | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ASP B 402 |
Chain | Residue |
B | THR168 |
B | GLY188 |
B | ARG196 |
B | ASP199 |
B | THR219 |
B | GLY220 |
B | GLY222 |
B | HOH504 |
B | HOH548 |
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 |