Structure of PDB 2qxx Chain B

Receptor sequence
>2qxxB (length=189) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
MLLSDRDLRAEISSGRLGIDPFDDTLVQPSSIDVRLDCLFRVFNNTRYTH
IDPAKQQDELTSLVQPVDGEPFVLHPGEFVLGSTLELFTLPDNLAGRLEG
KSSLGRLGLLTHSTAGFIDPGFSGHITLELSNVANLPITLWPGMKIGQLC
MLRLTSPSEHPYGSSRAGSKYQGQRGPTPSRSYQNFIRS
3D structure
PDB2qxx Mechanism of dTTP inhibition of the bifunctional dCTP deaminase:dUTPase encoded by Mycobacterium tuberculosis.
ChainB
Resolution2.0 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) S102 R106 A115 F117 E129
Catalytic site (residue number reindexed from 1) S102 R106 A115 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 B A115 G116 F117 D119 F122 I126 T127 Y162 S169 K170 A115 G116 F117 D119 F122 I126 T127 Y162 S169 K170
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2qxx, PDBe:2qxx, PDBj:2qxx
PDBsum2qxx
PubMed18164314
UniProtP9WP17|DCDB_MYCTU dCTP deaminase, dUMP-forming (Gene Name=dcd)

[Back to BioLiP]