Structure of PDB 7tu7 Chain A

Receptor sequence
>7tu7A (length=431) Species: 398720 (Leeuwenhoekiella blandensis MED217) [Search protein sequence]
NWEHLLSLKRQGDTAKRLRIEQLGFEVDYDRIIFSAPFRSLQDKTQVIPL
SKTDFVHTRLTHSLEVSVVGRSLGRMVGKKLLEKYPHLEQVYGYKFNDFG
AIVAAAALAHDIGNPPFGASGEKAIGEFFKNGYGKRYKDSLTAKEYQDLI
KFEGNANGFKVLSQSKPGAQGGLRLSYATLGAFMKYPKESLPHKPSDHIA
DKKYGFFQSERALFEDVAQELGLLKRSTTDDVSWSRHPLAYLVEAADDIC
YTIIDFEDGINLGLIPEEYALEYMVKLVGQTIDRNKYNALQETSDRVSYL
RALAIGTLINESVDTFMKYEEEILAGTFDQSLIDKSNYQAQITDIINLSI
ERIYNSREVIEKEIAGYEILSTLLEARCRALDNNDTHYNQLIQQLLAPEK
SLYENLIQICAEVSTMTDGKALRNYKKIKGL
3D structure
PDB7tu7 High-resolution structures of the SAMHD1 dGTPase homolog from Leeuwenhoekiella blandensis reveal a novel mechanism of allosteric activation by dATP.
ChainA
Resolution2.5 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 DGT A Q52 V53 K191 D253 D261 Q46 V47 K185 D247 D255
BS02 MG A H68 H116 D117 D253 H62 H110 D111 D247
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:7tu7, PDBe:7tu7, PDBj:7tu7
PDBsum7tu7
PubMed35643313
UniProtA3XHN1

[Back to BioLiP]