Structure of PDB 1mrn Chain A

Receptor sequence

>1mrnA (length=208) Species: 1773 (Mycobacterium tuberculosis)

MLIAIEGVDGAGKRTLVEKLSGAFRAAGRSVATLAFPRYGQSVAADIAAE
ALHGEHGDLASSVYAMATLFALDRAGAVHTIQGLCRGYDVVILDRYVASN
AAYSAARLHENAAGKAAAWVQRIEFARLGLPKPDWQVLLAVSAELAGERS
RGRAQRDPGRARDNYERDAELQQRTGAVYAELAAQGWGGRWLVVGADVDP
GRLAATLA

3D structure

• PDB: 1mrn Enzymatic and structural analysis of inhibitors designed against Mycobacterium tuberculosis thymidylate kinase. New insights into the phosphoryl transfer mechanism.
• Chain: A
• Resolution: 2.45 Å

Enzymatic activity

• Enzyme Commision number: 2.7.4.9: dTMP kinase.

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	MG	A	D9 E166	D9 E166
BS02	T5A	A	D9 F36 P37 Y39 A49 E50 H53 F70 R74 R95 S99 N100 Y103 R160 Y165	D9 F36 P37 Y39 A49 E50 H53 F70 R74 R95 S99 N100 Y103 R160 Y165	MOAD: Ki=30uM PDBbind-CN: -logKd/Ki=4.52,Ki=30uM

Gene Ontology

Molecular Function

• GO:0000287 magnesium ion binding
• GO:0004798 thymidylate kinase activity
• GO:0005524 ATP binding
• GO:0005525 GTP binding
• GO:0016301 kinase activity
• GO:0042803 protein homodimerization activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006227 dUDP biosynthetic process
• GO:0006233 dTDP biosynthetic process
• GO:0006235 dTTP biosynthetic process
• GO:0009165 nucleotide biosynthetic process
• GO:0016310 phosphorylation
• GO:0046044 TMP metabolic process
• GO:0046940 nucleoside monophosphate phosphorylation

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:1mrn, PDBe:1mrn, PDBj:1mrn
• PDBsum: 1mrn
• PubMed: 12454011
• UniProt: P9WKE1|KTHY_MYCTU Thymidylate kinase (Gene Name=tmk)