Structure of PDB 4lrl Chain C

Receptor sequence
>4lrlC (length=455) Species: 226185 (Enterococcus faecalis V583) [Search protein sequence]
TIPYKEQRLPIEKVFRDPVHNYIHVQHQVILDLINSAEVQRLRRIKQLGT
SSFTFHGAEHSRFSHSLGVYEITRRICEIFQRNYSVERLGENGWNDDERL
ITLCAALLHDVGHGPYSHTFEHIFDTNHEAITVQIITSPETEVYQILNRV
SADFPEKVASVITKQYPNPQVVQMISSQIDADRMDYLLRDAYFTGTEYGT
FDLTRILRVIRPYKGGIAFAMNGMHAVEDYIVSRYQMYVQVYFHPVSRGM
EVILDHLLHRAKELFENPEFDYDLQASLLVPFFKGDFTLQEYLKLDDGVL
STYFTQWMDVPDSILGDLAKRFLMRKPLKSATFTNEKESAATIAYLRELI
EKVGFNPKYYTAINSSYDLPYDFYRPNKDRHRTQIELMQKDGSLVELATV
SPLVAALAGQSQGDERFYFPKEMLDQGNKKHYDLFDETYREFSSYIHNGA
LVLKK
3D structure
PDB4lrl Mechanisms of Allosteric Activation and Inhibition of the Deoxyribonucleoside Triphosphate Triphosphohydrolase from Enterococcus faecalis.
ChainC
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 C K14 V15 F16 N36 R44 K13 V14 F15 N35 R43
BS02 DGT C F54 T55 V247 R326 K330 F53 T54 V246 R325 K329
BS03 TTP C T55 F56 Q241 H245 T54 F55 Q240 H244
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0008832 dGTPase activity
GO:0046872 metal ion binding
Biological Process
GO:0006203 dGTP catabolic process

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

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