1RPT
CRYSTAL STRUCTURES OF RAT ACID PHOSPHATASE COMPLEXED WITH THE TRANSITIONS STATE ANALOGS VANADATE AND MOLYBDATE: IMPLICATIONS FOR THE REACTION MECHANISM
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003993 | molecular_function | acid phosphatase activity |
| A | 0004725 | molecular_function | protein tyrosine phosphatase activity |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005765 | cellular_component | lysosomal membrane |
| A | 0005771 | cellular_component | multivesicular body |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006144 | biological_process | purine nucleobase metabolic process |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006772 | biological_process | thiamine metabolic process |
| A | 0008253 | molecular_function | 5'-nucleotidase activity |
| A | 0009117 | biological_process | nucleotide metabolic process |
| A | 0012506 | cellular_component | vesicle membrane |
| A | 0016020 | cellular_component | membrane |
| A | 0016311 | biological_process | dephosphorylation |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016791 | molecular_function | phosphatase activity |
| A | 0030141 | cellular_component | secretory granule |
| A | 0030175 | cellular_component | filopodium |
| A | 0031985 | cellular_component | Golgi cisterna |
| A | 0033265 | molecular_function | choline binding |
| A | 0042131 | molecular_function | thiamine phosphate phosphatase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0045177 | cellular_component | apical part of cell |
| A | 0046085 | biological_process | adenosine metabolic process |
| A | 0051930 | biological_process | regulation of sensory perception of pain |
| A | 0052642 | molecular_function | lysophosphatidic acid phosphatase activity |
| A | 0060090 | molecular_function | molecular adaptor activity |
| A | 0060168 | biological_process | positive regulation of adenosine receptor signaling pathway |
| A | 1904097 | cellular_component | acid phosphatase complex |
Functional Information from PROSITE/UniProt
| site_id | PS00616 |
| Number of Residues | 15 |
| Details | HIS_ACID_PHOSPHAT_1 Histidine acid phosphatases phosphohistidine signature. LkfVtlVfRHGdRgP |
| Chain | Residue | Details |
| A | LEU3-PRO17 |
| site_id | PS00778 |
| Number of Residues | 17 |
| Details | HIS_ACID_PHOSPHAT_2 Histidine acid phosphatases active site signature. LiMYsAHDTTVsgLqmA |
| Chain | Residue | Details |
| A | LEU251-ALA267 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"8077215","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"8077215","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P15309","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Important for substrate specificity","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Site: {"description":"Required for dimerization","evidences":[{"source":"PubMed","id":"8077215","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Site: {"description":"Required for structural stability","evidences":[{"source":"UniProtKB","id":"P15309","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"8334986","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8407898","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | a catalytic site defined by CSA, PubMed 8168503, 8993313, 9164457 |
| Chain | Residue | Details |
| A | ARG15 | |
| A | HIS257 | |
| A | ARG79 | |
| A | ASP258 | |
| A | ARG11 | |
| A | HIS12 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 454 |
| Chain | Residue | Details |
| A | ARG11 | electrostatic stabiliser |
| A | HIS12 | covalent catalysis |
| A | ARG15 | electrostatic stabiliser |
| A | ARG79 | electrostatic stabiliser |
| A | HIS257 | electrostatic stabiliser |
| A | ASP258 | electrostatic stabiliser, proton shuttle (general acid/base) |
