Structure of PDB 1kej Chain A

Receptor sequence
>1kejA (length=357) Species: 10090 (Mus musculus) [Search protein sequence]
KKISQYACQRRTTLNNYNQLFTDALDILAENDELRENEGSCLAFMRASSV
LKSLPFPITSMKDTEGIPCLGDKVKSIIEGIIEDGESSEAKAVLNDERYK
SFKLFTSVFGVGLKTAEKWFRMGFRTLSKIQSDKSLRFTQMQKAGFLYYE
DLVSCVNRPEAEAVSMLVKEAVVTFLPDALVTMTGGFRRGKMTGHDVDFL
ITSPEATEDEEQQLLHKVTDFWKQQGLLLYCDILESTFEQPSRKVDALDH
FQKCFLILKLDHGRVHSEKSEGKGWKAIRVDLVMCPYDRRAFALLGWTGS
RQFERDLRRYATHERKMMLDNHALYDRTKRVFLEAESEEEIFAHLGLDYI
EPWERNA
3D structure
PDB1kej Crystal structures of a template-independent DNA polymerase: murine terminal deoxynucleotidyltransferase.
ChainA
Resolution3.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D343 D345 D434
Catalytic site (residue number reindexed from 1) D196 D198 D281
Enzyme Commision number 2.7.7.31: DNA nucleotidylexotransferase.
3.1.11.-
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 CO A D343 D345 D196 D198
BS02 CO A D343 D345 D434 D196 D198 D281
BS03 DAD A G333 R336 G341 H342 D343 D345 R454 G186 R189 G194 H195 D196 D198 R301
Gene Ontology
Molecular Function
GO:0003677 DNA binding
GO:0003887 DNA-directed DNA polymerase activity
GO:0016779 nucleotidyltransferase activity
GO:0034061 DNA polymerase activity
Biological Process
GO:0006281 DNA repair

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Molecular Function
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Biological Process
External links
PDB RCSB:1kej, PDBe:1kej, PDBj:1kej
PDBsum1kej
PubMed11823435
UniProtP09838|TDT_MOUSE DNA nucleotidylexotransferase (Gene Name=Dntt)

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