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1KA0

The PAPase Hal2p complexed with a sodium ion and the reaction product AMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000103biological_processsulfate assimilation
A0005575cellular_componentcellular_component
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0006790biological_processsulfur compound metabolic process
A0008441molecular_function3'(2'),5'-bisphosphate nucleotidase activity
A0009086biological_processmethionine biosynthetic process
A0016078biological_processtRNA decay
A0016787molecular_functionhydrolase activity
A0042538biological_processhyperosmotic salinity response
A0046854biological_processphosphatidylinositol phosphate biosynthetic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NA A 501
ChainResidue
AGLU72
AASP142
AILE144
AHOH539
AHOH774

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE AMP A 401
ChainResidue
ALYS267
AARG281
ATYR288
AGLU290
AASP294
AHOH516
AHOH532
AHOH550
AHOH564
AHOH641
AHOH701
AHOH774
AGLY240
AHIS241
AASP263
ASER264

Functional Information from PROSITE/UniProt
site_idPS00629
Number of Residues14
DetailsIMP_1 Inositol monophosphatase family signature 1. WcLDPIDGTkgFlR
ChainResidueDetails
ATRP139-ARG152

site_idPS00630
Number of Residues15
DetailsIMP_2 Inositol monophosphatase family signature 2. WDhAAGnVIVheaGG
ChainResidueDetails
ATRP293-GLY307

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"12126627","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10656801","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12126627","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1K9Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QGX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12126627","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1K9Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KA1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12126627","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1KA1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10656801","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12126627","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2001","submissionDatabase":"PDB data bank","title":"Hal2p: Ion selectivity and implications on inhibition mechanism.","authors":["Patel S.","Albert A.","Blundell T.L."]}},{"source":"PDB","id":"1K9Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1KA0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1QGX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ima
ChainResidueDetails
ATHR147
AGLU72

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ima
ChainResidueDetails
ALYS32
ATHR147

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ima
ChainResidueDetails
AASP294
AASP49
ATHR147

site_idMCSA1
Number of Residues7
DetailsM-CSA 904
ChainResidueDetails
AASP49proton acceptor, proton donor
AGLU72metal ligand
AASP142metal ligand
AILE144metal ligand
AASP145metal ligand
ATHR147proton acceptor, proton donor, proton relay
AASP294metal ligand

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PDB entries from 2025-12-24

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