Structure of PDB 7tu8 Chain E

Receptor sequence
>7tu8E (length=434) Species: 398720 (Leeuwenhoekiella blandensis MED217) [Search protein sequence]
NWEHLLSLKRQGDTAKRLRIEQDDTRLGFEVDYDRIIFSAPFRSLQDKTQ
VIPLSKDFVHTRLTHSLEVSVVGRSLGRMVGKKLLEKYPHLEQVYGYKFN
DFGAIVAAAALAHDIGNPPFGASGEKAIGEFFKNGYGKRYKDSLTAKEYQ
DLIKFEGNANGFKVLSQSKPGAQGGLRLSYATLGAFMKYPKESLPHKPSD
HIADKKYGFFQSERALFEDVAQELGLLKRSTTDDVSWSRHPLAYLVEAAD
DICYTIIDFEDGINLGLIPEEYALEYMVKLVGQTIDRNKYNALQETSDRV
SYLRALAIGTLINESVDTFMKYEEEILAGTFDQSLIDKSNYQAQITDIIN
LSIERIYNSREVIEKEIAGYEILSTLLEARCRALDNNDTHYNQLIQQLLA
PEKSLYENLIQICAEVSTMTDGKALRNYKKIKGL
3D structure
PDB7tu8 High-resolution structures of the SAMHD1 dGTPase homolog from Leeuwenhoekiella blandensis reveal a novel mechanism of allosteric activation by dATP.
ChainE
Resolution2.6 Å
3D
structure
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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 E Q52 V53 Y257 D261 Y360 E369 Q50 V51 Y254 D258 Y357 E366
BS02 DTP E R28 R37 R26 R35
BS03 MG E H68 H116 D117 D253 H65 H113 D114 D250
BS04 DTP E S78 A308 I315 S75 A305 I312
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:7tu8, PDBe:7tu8, PDBj:7tu8
PDBsum7tu8
PubMed35643313
UniProtA3XHN1

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