Structure of PDB 1p72 Chain A

Receptor sequence
>1p72A (length=323) Species: 10331 (Equid alphaherpesvirus 4) [Search protein sequence]
SHMVTIVRIYLDGVYGIGKSTTGRVMASAASGGSPTLYFPEPMAYWRTLF
ETDVISGIYDTQNDAALITAHYQSRFTTPYLILHDHTCTLFGGNSLQRGT
QPDLTLVFDRHPVASTVCFPAARYLLGDMSMCALMAMVATLPREPQGGNI
VVTTLNVEEHIRRLRTRARIGEQIDITLIATLRNVYFMLVNTCHFLRSGR
VWRDGWGELPTSCGAYKHRATQMDAFQERVSPELGDTLFALFKTQELLDD
RGVILEVHAWALDALMLKLRNLNVFSADLSGTPRQCAAVVESLLPLMSST
LSDFDSASALERAARTFNAEMGV
3D structure
PDB1p72 Structural basis for the dual thymidine and thymidylate kinase activity of herpes thymidine kinases.
ChainA
Resolution2.1 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) K19 E41 D109 R110 R167 R169 E172
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 ADP A Y34 G35 G37 K38 S39 T40 R192 R196 P312 Y15 G16 G18 K19 S20 T21 R163 R167 P283
BS02 THM A Y34 I74 Y78 Q102 F105 S144 F148 Y15 I55 Y59 Q73 F76 S115 F119
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:1p72, PDBe:1p72, PDBj:1p72
PDBsum1p72
PubMed14527394
UniProtP24425|KITH_EHV4 Thymidine kinase (Gene Name=TK)

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