Structure of PDB 3lv8 Chain A

Receptor sequence

>3lv8A (length=204) Species: 243277 (Vibrio cholerae O1 biovar El Tor str. N16961)

NAKFIVIEGLEGAGKSTAIQVVVETLQQNGIDHITRTREPGGTLLAEKLR
ALVKEEHPGEELQDITELLLVYAARVQLVENVIKPALARGEWVVGDRHDM
SSQAYQGGGRQIAPSTMQSLKQTALGDFKPDLTLYLDIDPKLGLERELDR
IEKMDISFFERARERYLELANSDDSVVMIDAAQSIEQVTADIRRALQDWL
SQVN

3D structure

• PDB: 3lv8 1.8 Angstrom resolution crystal structure of a thymidylate kinase (tmk) from Vibrio cholerae O1 biovar eltor str. N16961 in complex with TMP, thymidine-5'-diphosphate and ADP
• Chain: A
• Resolution: 1.8 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	ADP	A	G13 G15 K16 S17 R147 Q189 I191	G12 G14 K15 S16 R146 Q183 I185
BS02	TMP	A	E12 E40 P41 K55 R76 R98 S102 S103 Y106 Q107 I157	E11 E39 P40 K54 R75 R97 S101 S102 Y105 Q106 I151
BS03	TYD	A	E12 E40 P41 K55 V72 R76 R98 S102 S103 Y106 Q107	E11 E39 P40 K54 V71 R75 R97 S101 S102 Y105 Q106
BS04	CA	A	E12 E158	E11 E152
BS05	CA	A	A176 D179 D180 V182	A170 D173 D174 V176

Gene Ontology

Molecular Function

• GO:0004712 protein serine/threonine/tyrosine kinase activity
• GO:0004798 thymidylate kinase activity
• GO:0005524 ATP binding
• GO:0016301 kinase activity

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:0046940 nucleoside monophosphate phosphorylation

Cellular Component

• GO:0005737 cytoplasm
• GO:0005829 cytosol

External links

• PDB: RCSB:3lv8, PDBe:3lv8, PDBj:3lv8
• PDBsum: 3lv8
• UniProt: Q9KQI2|KTHY_VIBCH Thymidylate kinase (Gene Name=tmk)