4O0C
High resolution crystal structure of uncleaved human L-asparaginase protein
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 | 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 | 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 | 3 |
Details | BINDING SITE FOR RESIDUE NA A 402 |
Chain | Residue |
A | GLY10 |
A | HOH639 |
A | HOH646 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DMS A 403 |
Chain | Residue |
A | VAL275 |
A | ALA276 |
A | TRP285 |
A | HOH608 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL A 404 |
Chain | Residue |
A | MET1 |
A | ASN2 |
B | HOH590 |
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 | VAL108 |
B | MET109 |
B | THR112 |
B | HIS114 |
B | HOH540 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE NA B 403 |
Chain | Residue |
A | HOH664 |
B | SER88 |
B | HOH540 |
site_id | AC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMS B 404 |
Chain | Residue |
B | VAL275 |
B | ALA276 |
B | TRP285 |
site_id | AC9 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL B 405 |
Chain | Residue |
A | LYS103 |
B | MET1 |
B | ASN2 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:19839645, ECO:0000269|PubMed:22861376 |
Chain | Residue | Details |
A | THR168 | |
B | THR168 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: |
Chain | Residue | Details |
A | ARG196 | |
A | THR219 | |
B | ARG196 | |
B | THR219 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330 |
Chain | Residue | Details |
A | MET1 | |
B | MET1 |