Structure of PDB 2hqu Chain B

Receptor sequence
>2hquB (length=141) Species: 9606 (Homo sapiens) [Search protein sequence]
MQLRFARLSEHATAPTRGSARAAGYDLYSAYDYTIPPMEKAVVKTDIQIA
LPSGCYGRVAPRSGLAAKHFIDVGAGVIDEDYRGNVGVVLFNFGKEKFEV
KKGDRIAQLICERIFYPEIEEVQALDDTERGSGGFGSTGKN
3D structure
PDB2hqu Active site closure facilitates juxtaposition of reactant atoms for initiation of catalysis by human dUTPase.
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 B A98 G99 V100 I101 D102 Y105 G110 A75 G76 V77 I78 D79 Y82 G87 MOAD: Kd=7.2uM
PDBbind-CN: -logKd/Ki=5.14,Kd=7.2uM
BS02 DUP B R153 G157 F158 G159 S160 T161 R130 G134 F135 G136 S137 T138 MOAD: Kd=7.2uM
PDBbind-CN: -logKd/Ki=5.14,Kd=7.2uM
BS03 DUP B R85 S86 G87 Q131 R62 S63 G64 Q108 MOAD: Kd=7.2uM
PDBbind-CN: -logKd/Ki=5.14,Kd=7.2uM
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

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Molecular Function
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Biological Process
External links
PDB RCSB:2hqu, PDBe:2hqu, PDBj:2hqu
PDBsum2hqu
PubMed17880943
UniProtP33316|DUT_HUMAN Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial (Gene Name=DUT)

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