Structure of PDB 7tu2 Chain C

Receptor sequence
>7tu2C (length=430) Species: 398720 (Leeuwenhoekiella blandensis MED217) [Search protein sequence]
ANWEHLLSLKRQGDTAKRLRIEQDDTRLGFEVDYDAIIFSAPFRSLQDKT
QVIPDFVHTRLTHSLEVSVVGRSLGRMVGKKLLEKYPHLEQVYGYKFNDF
GAIVAAAALAHDIGNPPFGHSGEKAIGEFFKNGYGKRYKDSLTAKEYQDL
IKFEGNANGFKVLSQSKPGAQGGLRLSYATLGAFMKYPKESLPHKPSDHI
ADKKYGFFQSERALFEDVAQELGLLKRSTTDDVSWSRHPLAYLVEAADDI
CYTIIDFEDGINLGLIPEEYALEYMVKLVGQTIDRNKYNALQETSDRVSY
LRALAIGTLINESVDTFMKYEEEILAGTFDQSLIDKSNYQAQITDIINLS
IERIYNSREVIEKEIAGYEILSTLLEARCRALDNNDTHYNQLIQQLLAPS
LYENLIQICAEVSTMTDGKALRNYKKIKGL
3D structure
PDB7tu2 High-resolution structures of the SAMHD1 dGTPase homolog from Leeuwenhoekiella blandensis reveal a novel mechanism of allosteric activation by dATP.
ChainC
Resolution2.13 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 ?
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 MN C H68 H116 D117 D253 H63 H111 D112 D248
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:7tu2, PDBe:7tu2, PDBj:7tu2
PDBsum7tu2
PubMed35643313
UniProtA3XHN1

[Back to BioLiP]