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1K7K

crystal structure of RdgB- inosine triphosphate pyrophosphatase from E. coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0009117biological_processnucleotide metabolic process
A0009143biological_processnucleoside triphosphate catabolic process
A0009146biological_processpurine nucleoside triphosphate catabolic process
A0016787molecular_functionhydrolase activity
A0017111molecular_functionribonucleoside triphosphate phosphatase activity
A0035870molecular_functiondITP diphosphatase activity
A0036220molecular_functionITP diphosphatase activity
A0036222molecular_functionXTP diphosphatase activity
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A0047429molecular_functionnucleoside triphosphate diphosphatase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000305|PubMed:17976651
ChainResidueDetails
AASP69

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01405, ECO:0000269|PubMed:17976651, ECO:0007744|PDB:2Q16
ChainResidueDetails
ATHR8
APHE154
AHIS182

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01405
ChainResidueDetails
AGLU40
AASP69

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17976651, ECO:0007744|PDB:2Q16
ChainResidueDetails
ASER70
ALYS177

219140

PDB entries from 2024-05-01

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