Structure of PDB 1vyq Chain B

Receptor sequence

>1vyqB (length=140) Species: 36329 (Plasmodium falciparum 3D7)

MHLKIVCLSDEVREMYKNHKTHHEGDSGLDLFIVKDEVLKPKSTTFVKLG
IKAIALQYKSNYYYKNIVNTSFLLFPRSSISKTPLRLANSIGLIDAGYRG
EIIAALDNTSDQEYHIKKNDKLVQLVSFTGEPLSFELVEE

3D structure

• PDB: 1vyq Dutpase as a Platform for Antimalarial Drug Design: Structural Basis for the Selectivity of a Class of Nucleoside Inhibitors.
• Chain: B
• Resolution: 2.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): S27 R91 S93 L99 D109
• Catalytic site (residue number reindexed from 1): S27 R77 S79 L85 D95
• Enzyme Commision number: 3.6.1.23: dUTP diphosphatase.

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	DUX	B	S92 S93	S78 S79	MOAD: Ki=4.98uM PDBbind-CN: -logKd/Ki=5.30,Ki=4.98uM BindingDB: Ki=5000nM
BS02	DUX	B	G106 Y112 I117	G92 Y98 I103	MOAD: Ki=4.98uM PDBbind-CN: -logKd/Ki=5.30,Ki=4.98uM BindingDB: Ki=5000nM

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0004170 dUTP diphosphatase activity
• GO:0016787 hydrolase activity
• GO:0042802 identical protein binding
• GO:0046872 metal ion binding

Biological Process

• GO:0006226 dUMP biosynthetic process
• GO:0006260 DNA replication
• GO:0006399 tRNA metabolic process
• GO:0009117 nucleotide metabolic process
• GO:0046081 dUTP catabolic process

External links

• PDB: RCSB:1vyq, PDBe:1vyq, PDBj:1vyq
• PDBsum: 1vyq
• PubMed: 15698576
• UniProt: Q8II92