Structure of PDB 6rmw Chain F

Receptor sequence
>6rmwF (length=378) Species: 36329 (Plasmodium falciparum 3D7) [Search protein sequence]
IVQWNSRYSYNQLKNKDSLIMFLVEIFRSLFVSNCIDKNIDNVLLSIEEM
FIDHYYNPQHSRLKYLIDDVGIFFTKLPITKAFHTYNKKYRITKRLYAPP
TFNEVRHILNLAQILSLEEGLDLLTFDANETLYPDGHDFNDEVLASYISC
LLKKMNIAIVTAASYNNDAEKYQKRLENLLKYFSKHNIKDGSYKNFYVMG
GESNYLFKCNEEATLYSVPENEWRHYKKFVDYDTVQEILNISEKCLEKVI
KDFGLCAQIQRKEKSIGLVPNKINYMIKYEVLEEAVIRIKKEIIKNKITA
PYCAFNGGQDLWVDVGNKAEGLLILQKLLKIQKKKCCHIGDQFLHSGNDF
PTRFCSLTLWVSNPQETKACLKSIMHLN
3D structure
PDB6rmw Structure and catalytic regulation of Plasmodium falciparum IMP specific nucleotidase.
ChainF
Resolution3.5 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 3.1.3.99: IMP-specific 5'-nucleotidase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 IMP F D170 N172 T204 A205 A206 S207 K305 S308 D363 W365 N401 D127 N129 T161 A162 A163 S164 K262 S265 D310 W312 N348
BS02 MG F D170 N172 D394 D127 N129 D341
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0005524 ATP binding
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
GO:0050483 IMP 5'-nucleotidase activity
Biological Process
GO:0006190 inosine salvage
GO:0006204 IMP catabolic process
GO:0009117 nucleotide metabolic process
GO:0071590 nicotinamide riboside biosynthetic process
GO:0071592 nicotinic acid riboside biosynthetic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:6rmw, PDBe:6rmw, PDBj:6rmw
PDBsum6rmw
PubMed32591529
UniProtA0A144A134|ISN1_PLAF7 IMP-specific 5'-nucleotidase 1 (Gene Name=ISN1)

[Back to BioLiP]