Structure of PDB 3ehw Chain A

Receptor sequence
>3ehwA (length=141) Species: 9606 (Homo sapiens) [Search protein sequence]
MQLRFARLSEHATAPTRGSARAAGYDLYSAYDYTIPPMEKAVVKTDIQIA
LPSGCYGRVAPRSGLAAKHFIDVGAGVIDEDYRGNVGVVLFNFGKEKFEV
KKGDRIAQLICERIFYPEIEEVQALDDTERGSGGFGSTGKN
3D structure
PDB3ehw Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and active sites formed by three separate subunits.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) A46 R85 G87 I94 D102
Catalytic site (residue number reindexed from 1) A23 R62 G64 I71 D79
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 DUP A R153 G157 F158 G159 S160 T161 R130 G134 F135 G136 S137 T138 PDBbind-CN: -logKd/Ki=4.82,IC50=15.2uM
BS02 DUP A A98 G99 V100 I101 D102 Y105 G110 A75 G76 V77 I78 D79 Y82 G87 PDBbind-CN: -logKd/Ki=4.82,IC50=15.2uM
BS03 DUP A R85 S86 G87 R62 S63 G64 PDBbind-CN: -logKd/Ki=4.82,IC50=15.2uM
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004170 dUTP diphosphatase activity
Biological Process
GO:0006226 dUMP biosynthetic process
GO:0046081 dUTP catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3ehw, PDBe:3ehw, PDBj:3ehw
PDBsum3ehw
PubMed
UniProtP33316|DUT_HUMAN Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial (Gene Name=DUT)

[Back to BioLiP]