Structure of PDB 2hrm Chain A

Receptor sequence
>2hrmA (length=137) Species: 562 (Escherichia coli) [Search protein sequence]
MMKKIDVKILDPRVGKEFPLPTYATSGSAGLDLRACLNDAVELAPGDTTL
VPTGLAIHIADPSLAAMMLPRSGLGHKHGIVLGNLVGLIDSDYQGQLMIS
VWNRGQDSFTIQPGERIAQMIFVPVVQAEFNLVEDFD
3D structure
PDB2hrm Methylene substitution at the alpha-beta bridging position within the phosphate chain of dUDP profoundly perturbs ligand accommodation into the dUTPase active site.
ChainA
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) A29 R71 G73 I80 D90
Catalytic site (residue number reindexed from 1) A29 R71 G73 I80 D90
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 UC5 A N84 L88 I89 D90 Y93 M98 N84 L88 I89 D90 Y93 M98 MOAD: Kd=278.5uM
PDBbind-CN: -logKd/Ki=3.56,Kd=278.5uM
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:0009117 nucleotide metabolic process
GO:0046081 dUTP catabolic process
GO:0070207 protein homotrimerization
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol
GO:0032991 protein-containing complex

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Cellular Component
External links
PDB RCSB:2hrm, PDBe:2hrm, PDBj:2hrm
PDBsum2hrm
PubMed17932923
UniProtP06968|DUT_ECOLI Deoxyuridine 5'-triphosphate nucleotidohydrolase (Gene Name=dut)

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