Structure of PDB 1p73 Chain C

Receptor sequence
>1p73C (length=317) Species: 10331 (Equid alphaherpesvirus 4) [Search protein sequence]
MVTIVRIYLDGVYGIGKSTTGRVMASSPTLYFPEPMAYWRTLFETDVISG
IYDTQNRVDDAALITAHYQSRFTTPYLILHDHTCTLFGGNSLQRGTQPDL
TLVFDRHPVASTVCFPAARYLLGDMSMCALMAMVATLPREPQGGNIVVTT
LNVEEHIRRLRTRAREQIDITLIATLRNVYFMLVNTCHFLRSGRVWRDGW
GELPTSCGAYKHRATQMDAFQERVSPELGDTLFALFKTQELLDDRGVILE
VHAWALDALMLKLRNLNVFSADLSGTPRQCAAVVESLLPLMSSTLSDFDS
ASALERAARTFNAEMGV
3D structure
PDB1p73 Structural basis for the dual thymidine and thymidylate kinase activity of herpes thymidine kinases.
ChainC
Resolution2.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K38 E60 D138 R139 R196 R198 E201
Catalytic site (residue number reindexed from 1) K17 E34 D105 R106 R163 R165 E166
Enzyme Commision number 2.7.1.21: thymidine 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 4TA C Y34 G35 G37 K38 S39 T40 E60 Y78 Q102 F105 R139 S144 F148 R192 P312 Y13 G14 G16 K17 S18 T19 E34 Y52 Q69 F72 R106 S111 F115 R159 P277
Gene Ontology
Molecular Function
GO:0004797 thymidine kinase activity
GO:0005524 ATP binding
GO:0016301 kinase activity
Biological Process
GO:0006230 TMP biosynthetic process
GO:0009157 deoxyribonucleoside monophosphate biosynthetic process
GO:0016310 phosphorylation
GO:0071897 DNA biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:1p73, PDBe:1p73, PDBj:1p73
PDBsum1p73
PubMed14527394
UniProtP24425|KITH_EHV4 Thymidine kinase (Gene Name=TK)

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