Structure of PDB 1p75 Chain A

Receptor sequence
>1p75A (length=331) Species: 10331 (Equid alphaherpesvirus 4) [Search protein sequence]
HMVTIVRIYLDGVYGIGKSTTGRVMASAASGGSPTLYFPEPMAYWRTLFE
TDVISGIYDTQNRKQQGNLAVDDAALITAHYQSRFTTPYLILHDHTCTLF
GGNSLQRGTQPDLTLVFDRHPVASTVCFPAARYLLGDMSMCALMAMVATL
PREPQGGNIVVTTLNVEEHIRRLRTRARGEQIDITLIATLRNVYFMLVNT
CHFLRSGRVWRDGWGELPTSCGAYKHRATQMDAFQERVSPELGDTLFALF
KTQELLDDRGVILEVHAWALDALMLKLRNLNVFSADLSGTPRQCAAVVES
LLPLMSSTLSDFDSASALERAARTFNAEMGV
3D structure
PDB1p75 Structural basis for the dual thymidine and thymidylate kinase activity of herpes thymidine kinases.
ChainA
Resolution3.02 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 E201
Catalytic site (residue number reindexed from 1) K18 E40 D118 R119 E180
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 T5A A Y34 G35 I36 G37 K38 S39 T40 E60 Y78 Q102 F105 R139 S144 F148 R192 P312 Y14 G15 I16 G17 K18 S19 T20 E40 Y58 Q82 F85 R119 S124 F128 R172 P291
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:1p75, PDBe:1p75, PDBj:1p75
PDBsum1p75
PubMed14527394
UniProtP24425|KITH_EHV4 Thymidine kinase (Gene Name=TK)

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