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6RN1

Structure of N-terminal truncated Plasmodium falciparum IMP-nucleotidase

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0006190biological_processinosine salvage
A0009117biological_processnucleotide metabolic process
A0050483molecular_functionIMP 5'-nucleotidase activity
B0000287molecular_functionmagnesium ion binding
B0006190biological_processinosine salvage
B0009117biological_processnucleotide metabolic process
B0050483molecular_functionIMP 5'-nucleotidase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Nucleophile => ECO:0000305|PubMed:32591529
ChainResidueDetails
AASP170
BASP170

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000305|PubMed:32591529
ChainResidueDetails
AASP172
BASP172

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:32591529, ECO:0007744|PDB:6RMD
ChainResidueDetails
ALYS132
AHIS150
BLYS132
BHIS150

site_idSWS_FT_FI4
Number of Residues18
DetailsBINDING: BINDING => ECO:0000269|PubMed:32591529, ECO:0007744|PDB:6RME, ECO:0007744|PDB:6RMW
ChainResidueDetails
AASP170
AASP172
AASP178
ATHR204
ASER207
ASER308
AASP363
ALYS371
AASP394
BASP170
BASP172
BASP178
BTHR204
BSER207
BSER308
BASP363
BLYS371
BASP394

221051

PDB entries from 2024-06-12

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