Structure of PDB 1kdh Chain A

Receptor sequence
>1kdhA (length=356) Species: 10090 (Mus musculus) [Search protein sequence]
KKISQYACQRRTTLNNYNQLFTDALDILAENDELRENEGSCLAFMRASSV
LKSLPFPITSMKDTEGIPCLGDKVKSIIEGIIEDGESSEAKAVLNDERYK
SFKLFTSVFGVGLKTAEKWFRMGFRTLSKIQSDKSLRFTQMQKAGFLYYE
DLVSCVNRPEAEAVSMLVKEAVVTFLPDALVTMTGGFRRGKMTGHDVDFL
ITSPEATEDEEQQLLHKVTDFWKQQGLLLYCDILESTFEKFKQPSRLDHF
QKCFLILKLDHGRVHSEKSEGKGWKAIRVDLVMCPYDRRAFALLGWTGSR
QFERDLRRYATHERKMMLDNHALYDRTKRVFLEAESEEEIFAHLGLDYIE
PWERNA
3D structure
PDB1kdh 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
Catalytic site (residue number reindexed from 1) D196 D198
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 dna A G257 V258 G259 K261 T262 R336 D345 F405 R432 D434 G449 W450 S453 R454 E457 G110 V111 G112 K114 T115 R189 D198 F254 R278 D280 G295 W296 S299 R300 E303
BS02 MG A D345 D434 W450 D198 D280 W296
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:1kdh, PDBe:1kdh, PDBj:1kdh
PDBsum1kdh
PubMed11823435
UniProtP09838|TDT_MOUSE DNA nucleotidylexotransferase (Gene Name=Dntt)

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