Structure of PDB 3irh Chain B

Receptor sequence
>3irhB (length=445) Species: 226185 (Enterococcus faecalis V583) [Search protein sequence]
MTIPYKEQRLPIEKVFRDPVHNYIHVQHQVILDLINSAEVQRLRRIKQLG
TSSFTFHGAEHSRFSHSLGVYEITRRICEIFQRNYSVERLGENGWNDDER
LITLCAALLHDVGHGPYSHTFEHIFDTNHEAITVQIITSPETEVYQILNR
VSADFPEKVASVITKQYPNPQVVQMISSQIDADRMDYLLRDAYFTGTEYG
TFDLTRILRVIRPYKGGIAFAMNGMHAVEDYIVSRYQMYVQVYFHPVSRG
MEVILDHLLHRAKELFENPEFDYDLQASLLVPFFKGDFTLQEYLKLDDGV
LSTYFTQWMDVPDSILGDLAKRFLMRKPLKSATFTNEKESAATIAYLREL
IEKVGFNPKYYTAINSSYDLPRTQIELMQKDGSLVELATVSPLVAALAGQ
SQGDERFYFPKEMLDQGNKKHYDLFDETYREFSSYIHNGALVLKK
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.
ChainB
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 B K14 V15 F16 N36 R44 K14 V15 F16 N36 R44
BS02 DGT B F54 T55 R326 K330 F54 T55 R326 K330
BS03 CA B H66 H110 D111 D183 H66 H110 D111 D183
BS04 DTP B L49 H119 Y187 Y239 Y243 Y368 L49 H119 Y187 Y239 Y243 Y368
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

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Biological Process
External links
PDB RCSB:3irh, PDBe:3irh, PDBj:3irh
PDBsum3irh
PubMed21757692
UniProtQ836G9

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