Structure of PDB 4a6a Chain K

Receptor sequence
>4a6aK (length=188) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
MLLSDRDLRAEISSGRLGIDPFDDTLVQPSSIDVRLDCLFRVFNNTRYTH
IDPAKQQDELTSLVQPVDGEPFVLHPGEFVLGSTLELFTLPDNLAGRLEG
KSSLGRLGLLTHSTVGFIDPGFSGHITLELSNVANLPITLWPGMKIGQLC
MLRLTSPSEHPYGSSRAGSKYQGQRGPTPSRSYQNFIR
3D structure
PDB4a6a Dttp Inhibition of the Bifunctional Dctp Deaminase- Dutpase from Mycobacterium Tuberculosis is Ph Dependent: Kinetic Analyses and Crystal Structure of A115V Variant
ChainK
Resolution2.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S102 R106 V115 F117 E129
Catalytic site (residue number reindexed from 1) S102 R106 V115 F117 E129
Enzyme Commision number 3.5.4.30: dCTP deaminase (dUMP-forming).
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 TTP K K101 S102 S103 K101 S102 S103
BS02 TTP K V115 G116 F117 D119 F122 T127 Y162 K170 Y171 V115 G116 F117 D119 F122 T127 Y162 K170 Y171
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004170 dUTP diphosphatase activity
GO:0008829 dCTP deaminase activity
GO:0016787 hydrolase activity
GO:0033973 dCTP deaminase (dUMP-forming) activity
Biological Process
GO:0006226 dUMP biosynthetic process
GO:0006229 dUTP biosynthetic process
GO:0009117 nucleotide metabolic process
GO:0015949 nucleobase-containing small molecule interconversion

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Molecular Function
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Biological Process
External links
PDB RCSB:4a6a, PDBe:4a6a, PDBj:4a6a
PDBsum4a6a
PubMed
UniProtP9WP17|DCDB_MYCTU dCTP deaminase, dUMP-forming (Gene Name=dcd)

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