Structure of PDB 3irh Chain D

Receptor sequence
>3irhD (length=434) Species: 226185 (Enterococcus faecalis V583) [Search protein sequence]
TIPYKEQRLPIEKVFRDPVHNYIHVQHQVILDLINSAEVQRLRRIKQLGT
SSFTFHGAEHSRFSHSLGVYEITRRICEIFQRNYSVERLGENGWNDDERL
ITLCAALLHDVGHGPYSHTFEHIFDTNHEAITVQIITSPETEVYQILNRV
SADFPEKVASVITKQYPNPQVVQMISSQIDADRMDYLLRDAYFTGTEYGT
FDLTRILRVIRPYKGGIAFAMNGMHAVEDYIVSRYQMYVQVYFHPVSRGM
EVILDHLLHRAKELFENPEFDYDLQASLLVPFFKGDFTLQEYLKLDDGVL
STYFTQWMDVPDSILGDLAKRFLMRKPLKSATFTNEKESAATIAYLRELI
EKVGFNPKYYTAINSSYDTQIELMQKDGSLVELATVSPLVAALAGQSQGD
ERFYFPKEMLDDLFDETYREFSSYIHNGALVLKK
3D structure
PDB3irh Characterization of the deoxynucleotide triphosphate triphosphohydrolase (dNTPase) activity of the EF1143 protein from Enterococcus faecalis and crystal structure of the activator-substrate complex.
ChainD
Resolution2.4 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 D K14 F16 N36 R44 K13 F15 N35 R43
BS02 DGT D F54 T55 V247 R326 F53 T54 V246 R325
BS03 CA D H66 H110 D111 D183 H65 H109 D110 D182
BS04 DTP D L49 S52 H114 H119 Y187 Y239 Y243 Y368 D369 L48 S51 H113 H118 Y186 Y238 Y242 Y367 D368
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
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Biological Process
External links
PDB RCSB:3irh, PDBe:3irh, PDBj:3irh
PDBsum3irh
PubMed21757692
UniProtQ836G9

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