1RPA
THREE-DIMENSIONAL STRUCTURE OF RAT ACID PHOSPHATASE IN COMPLEX WITH L(+) TARTRATE
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 | 0005764 | cellular_component | lysosome |
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 | 0007040 | biological_process | lysosome organization |
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 | 0106411 | molecular_function | XMP 5'-nucleosidase activity |
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 | ACT_SITE: Nucleophile => ECO:0000269|PubMed:8077215 |
Chain | Residue | Details |
A | HIS12 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:8077215 |
Chain | Residue | Details |
A | ASP258 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P15309 |
Chain | Residue | Details |
A | ARG11 | |
A | ARG15 | |
A | ARG79 | |
A | HIS257 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Important for substrate specificity => ECO:0000250 |
Chain | Residue | Details |
A | PRO17 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | SITE: Required for dimerization => ECO:0000269|PubMed:8077215 |
Chain | Residue | Details |
A | TRP106 | |
A | HIS112 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | SITE: Required for structural stability => ECO:0000250|UniProtKB:P15309 |
Chain | Residue | Details |
A | TRP174 |
site_id | SWS_FT_FI7 |
Number of Residues | 2 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8334986, ECO:0000269|PubMed:8407898 |
Chain | Residue | Details |
A | ASN62 | |
A | ASN301 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN188 |
Catalytic Information from CSA
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) |