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1RPA

THREE-DIMENSIONAL STRUCTURE OF RAT ACID PHOSPHATASE IN COMPLEX WITH L(+) TARTRATE

Functional Information from GO Data
ChainGOidnamespacecontents
A0003993molecular_functionacid phosphatase activity
A0004725molecular_functionprotein tyrosine phosphatase activity
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005764cellular_componentlysosome
A0005765cellular_componentlysosomal membrane
A0005771cellular_componentmultivesicular body
A0005886cellular_componentplasma membrane
A0006144biological_processpurine nucleobase metabolic process
A0006629biological_processlipid metabolic process
A0006772biological_processthiamine metabolic process
A0007040biological_processlysosome organization
A0008253molecular_function5'-nucleotidase activity
A0009117biological_processnucleotide metabolic process
A0012506cellular_componentvesicle membrane
A0016020cellular_componentmembrane
A0016311biological_processdephosphorylation
A0016787molecular_functionhydrolase activity
A0016791molecular_functionphosphatase activity
A0030141cellular_componentsecretory granule
A0030175cellular_componentfilopodium
A0031985cellular_componentGolgi cisterna
A0033265molecular_functioncholine binding
A0042131molecular_functionthiamine phosphate phosphatase activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0045177cellular_componentapical part of cell
A0046085biological_processadenosine metabolic process
A0051930biological_processregulation of sensory perception of pain
A0052642molecular_functionlysophosphatidic acid phosphatase activity
A0060090molecular_functionmolecular adaptor activity
A0060168biological_processpositive regulation of adenosine receptor signaling pathway
A0106411molecular_functionXMP 5'-nucleosidase activity
Functional Information from PROSITE/UniProt
site_idPS00616
Number of Residues15
DetailsHIS_ACID_PHOSPHAT_1 Histidine acid phosphatases phosphohistidine signature. LkfVtlVfRHGdRgP
ChainResidueDetails
ALEU3-PRO17

site_idPS00778
Number of Residues17
DetailsHIS_ACID_PHOSPHAT_2 Histidine acid phosphatases active site signature. LiMYsAHDTTVsgLqmA
ChainResidueDetails
ALEU251-ALA267

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:8077215
ChainResidueDetails
AHIS12

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:8077215
ChainResidueDetails
AASP258

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P15309
ChainResidueDetails
AARG11
AARG15
AARG79
AHIS257

site_idSWS_FT_FI4
Number of Residues1
DetailsSITE: Important for substrate specificity => ECO:0000250
ChainResidueDetails
APRO17

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Required for dimerization => ECO:0000269|PubMed:8077215
ChainResidueDetails
ATRP106
AHIS112

site_idSWS_FT_FI6
Number of Residues1
DetailsSITE: Required for structural stability => ECO:0000250|UniProtKB:P15309
ChainResidueDetails
ATRP174

site_idSWS_FT_FI7
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:8334986, ECO:0000269|PubMed:8407898
ChainResidueDetails
AASN62
AASN301

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN188

Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 454
ChainResidueDetails
AARG11electrostatic stabiliser
AHIS12covalent catalysis
AARG15electrostatic stabiliser
AARG79electrostatic stabiliser
AHIS257electrostatic stabiliser
AASP258electrostatic stabiliser, proton shuttle (general acid/base)

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PDB entries from 2024-04-17

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