Structure of PDB 7tu2 Chain A

Receptor sequence
>7tu2A (length=434) Species: 398720 (Leeuwenhoekiella blandensis MED217) [Search protein sequence]
ANWEHLLSLKRQGDTAKRLRIEQDDTRLGFEVDYDAIIFSAPFRSLQDKT
QVIPLSKTDFVHTRLTHSLEVSVVGRSLGRMVGKKLLEKYPHLEQVYGYK
FNDFGAIVAAAALAHDIGNPPFGHSGEKAIGEFFKNGYGKRYKDSLTAKE
YQDLIKFEGNANGFKVLSQSKPGAQGGLRLSYATLGAFMKYPKESLPHKP
SDHIADKKYGFFQSERALFEDVAQELGLLKRSTTDDVSWSRHPLAYLVEA
ADDICYTIIDFEDGINLGLIPEEYALEYMVKLVGQTIDRNKYNALQETSD
RVSYLRALAIGTLINESVDTFMKYEEEILAGTFDQSLIDKSNYQAQITDI
INLSIERIYNSREVIEKEIAGYEILSTLLEARCRALDNNDTHYNQLIQQL
LAPSLYENLIQICAEVSTMTDGKALRNYKKIKGL
3D structure
PDB7tu2 High-resolution structures of the SAMHD1 dGTPase homolog from Leeuwenhoekiella blandensis reveal a novel mechanism of allosteric activation by dATP.
ChainA
Resolution2.13 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 MN A H68 H116 D117 D253 H67 H115 D116 D252
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

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Molecular Function
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Biological Process
External links
PDB RCSB:7tu2, PDBe:7tu2, PDBj:7tu2
PDBsum7tu2
PubMed35643313
UniProtA3XHN1

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