Structure of PDB 4lrl Chain D

Receptor sequence
>4lrlD (length=439) Species: 226185 (Enterococcus faecalis V583) [Search protein sequence]
MTIPYKEQRLPIEKVFRDPVHNYIHVQHQVILDLINSAEVQRLRRIKQLG
TSSFTFHGAEHSRFSHSLGVYEITRRICEIFQRNYSVERLGENGWNDDER
LITLCAALLHDVGHGPYSHTFEHIFDTNHEAITVQIITSPETEVYQILNR
VSADFPEKVASVITKQYPNPQVVQMISSQIDADRMDYLLRDAYFTGTEYG
TFDLTRILRVIRPYKGGIAFAMNGMHAVEDYIVSRYQMYVQVYFHPVSRG
MEVILDHLLHRAKELFENPEFDYDLQASLLVPFFKGDFTLQEYLKLDDGV
LSTYFTQWMDVPDSILGDLAKRFLMRKPLKSATFTNEKESAATIAYLREL
IEKVGFNPKYYTAINSSYDLPYDFYRPNKDRHRTQIELMQKDGSLVELAT
VSPLVAALAGQSQGDERFYFPKEMLDLFDETYREFSSYI
3D structure
PDB4lrl Mechanisms of Allosteric Activation and Inhibition of the Deoxyribonucleoside Triphosphate Triphosphohydrolase from Enterococcus faecalis.
ChainD
Resolution2.35 Å
3D
structure
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Enzymatic activity
Enzyme Commision number ?
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 TTP D R206 R209 R206 R209
BS02 DGT D F54 T55 R326 K330 K422 F54 T55 R326 K330 K422
BS03 DGT D K14 V15 F16 N36 R44 K14 V15 F16 N36 R44
BS04 TTP D V15 R17 V15 R17
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0008832 dGTPase activity
GO:0046872 metal ion binding
Biological Process
GO:0006203 dGTP catabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4lrl, PDBe:4lrl, PDBj:4lrl
PDBsum4lrl
PubMed24338016
UniProtQ836G9

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