Structure of PDB 7tu6 Chain B

Receptor sequence
>7tu6B (length=430) Species: 398720 (Leeuwenhoekiella blandensis MED217) [Search protein sequence]
NWEHLLSLKRQGDTAKRLRIEQDDTRLGFEVDYDRIIFSAPFRSLQDKTQ
VIPLDFVHTRLTHSLEVSVVGRSLGRMVGKKLLEKYPHLEQVYGYKFNDF
GAIVAAAALAHDIGNPPFGHSGEKAIGEFFKNGYGKRYKDSLTAKEYQDL
IKFEGNANGFKVLSQSKPGAQGGLRLSYATLGAFMKYPKESLPHKPSDHI
ADKKYGFFQSERALFEDVAQELGLLKRSDVSWSRHPLAYLVEAADDICYT
IIDFEDGINLGLIPEEYALEYMVKLVGQTIDRNKYNALQETSDRVSYLRA
LAIGTLINESVDTFMKYEEEILAGTFDQSLIDKSNYQAQITDIINLSIER
IYNSREVIEKEIAGYEILSTLLEARCRALDNNDTHYNQLIQQLLAPNEKS
LYENLIQICAEVSTMTDGKALRNYKKIKGL
3D structure
PDB7tu6 High-resolution structures of the SAMHD1 dGTPase homolog from Leeuwenhoekiella blandensis reveal a novel mechanism of allosteric activation by dATP.
ChainB
Resolution2.7 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 3.1.5.1: dGTPase.
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 DTP B S78 A308 I315 S73 A300 I307
BS02 DTP B R28 R37 R26 R35
BS03 DTP B Q52 D261 Q50 D253
BS04 MG B H68 H116 D117 D253 H63 H111 D112 D245
Gene Ontology
Molecular Function
GO:0008832 dGTPase activity
GO:0016787 hydrolase activity
GO:0016793 triphosphoric monoester hydrolase 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:7tu6, PDBe:7tu6, PDBj:7tu6
PDBsum7tu6
PubMed35643313
UniProtA3XHN1

[Back to BioLiP]