Structure of PDB 1p6x Chain B

Receptor sequence
>1p6xB (length=331) Species: 10331 (Equid alphaherpesvirus 4) [Search protein sequence]
HMVTIVRIYLDGVYGIGKSTTGRVMASAASGGSPTLYFPEPMAYWRTLFE
TDVISGIYDTQNRKQQGNLAVDDAALITAHYQSRFTTPYLILHDHTCTLF
GGNSLQRGTQPDLTLVFDRHPVASTVCFPAARYLLGDMSMCALMAMVATL
PREPQGGNIVVTTLNVEEHIRRLRTRARIGEQIDITLIATLRNVYFMLVN
TCHFLRSGRVWRDGWGELPTSCGAYKHRATQMDAFQERVSPELGDTLFAL
FKTQELLDDRGVILEVHAWALDALMLKLRNLNVFSADLSGTPRQCAAVVE
SLLPLMSSTLSDFDSASALERAARTFNAEMG
3D structure
PDB1p6x Structural basis for the dual thymidine and thymidylate kinase activity of herpes thymidine kinases.
ChainB
Resolution2.0 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) K18 E40 D118 R119 R176 R178 E181
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 THM B Y34 E60 W65 Q102 F105 S144 F148 E201 Y14 E40 W45 Q82 F85 S124 F128 E181
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:1p6x, PDBe:1p6x, PDBj:1p6x
PDBsum1p6x
PubMed14527394
UniProtP24425|KITH_EHV4 Thymidine kinase (Gene Name=TK)

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