Structure of PDB 4lrl Chain A

Receptor sequence
>4lrlA (length=451) Species: 226185 (Enterococcus faecalis V583) [Search protein sequence]
AMTIPYKEQRLPIEKVFRDPVHNYIHVQHQVILDLINSAEVQRLRRIKQL
GTSSFTFHGAEHSRFSHSLGVYEITRRICEIFQRNYSVERLGENGWNDDE
RLITLCAALLHDVGHGPYSHTFEHIFDTNHEAITVQIITSPETEVYQILN
RVSADFPEKVASVITKQYPNPQVVQMISSQIDADRMDYLLRDAYFTGTEY
GTFDLTRILRVIRPYKGGIAFAMNGMHAVEDYIVSRYQMYVQVYFHPVSR
GMEVILDHLLHRAKELFENPEFDYDLQASLLVPFFKGDFTLQEYLKLDDG
VLSTYFTQWMDVPDSILGDLAKRFLMRKPLKSATFTNEKESAATIAYLRE
LIEKVGFNPKYYTAINSSYDLPYDFYRPNKDRHRTQIELMQKDGSLVELA
TVSPLVAALAGQSQGDERFYFPKEMLDQDLFDETYREFSSYIHNGALVLK
K
3D structure
PDB4lrl Mechanisms of Allosteric Activation and Inhibition of the Deoxyribonucleoside Triphosphate Triphosphohydrolase from Enterococcus faecalis.
ChainA
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 DGT A K14 V15 F16 N36 R44 K15 V16 F17 N37 R45
BS02 DGT A F54 T55 R326 F55 T56 R327
BS03 TTP A T55 F56 Q241 H245 T56 F57 Q242 H246
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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