Structure of PDB 7u67 Chain F

Receptor sequence
>7u67F (length=476) Species: 511145 (Escherichia coli str. K-12 substr. MG1655) [Search protein sequence]
QIDFRKKINWHRRYRSPQGVKTEHEILRIFESDRGRIINSPAIRRLQQKT
QVFPAVRTRLTHSMEVQQVGRYIAKEILSRLKELKLLEAYGLDELTGPFE
SIVEMSCLMHDIGNPPFGHFGEAAINDWFRQRLHPEDAESQPLDRCSVAA
LRLREEPLNELRRKIRQDLCHFEGNAQGIRLVHTLMRMNLTWAQVGGILK
YTRPAWWRGETPETHHYLMKKPGYYLSEEAYIARLRKELNLALYSRFPLT
WIMEAADDISYCVADLEDAVEKRIFTVEQLYHHLHEAWGFSLVVENAWEK
STEDQFFMYLRVNTLNKLVPYAAQRFIDNLPAIFAGTFNHALLASECSDL
LKLYKNVAVKHVFSHPDVERLELQGYRVISGLLEIYRPLLSLSLSDFTEL
VEKERVKRFPIESRLFHKLSTRHRLAYVEAVSKLPSDSPEFPLWEYYYRC
RLLQDYISGMTDLYAWDEYRRLMAVE
3D structure
PDB7u67 Mechanism by which T7 bacteriophage protein Gp1.2 inhibits Escherichia coli dGTPase.
ChainF
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 GTP F Q53 K232 Y272 F391 Q51 K221 Y261 F363
BS02 MG F H69 H117 D268 H62 H110 D257
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0003697 single-stranded DNA binding
GO:0003924 GTPase activity
GO:0008832 dGTPase activity
GO:0016787 hydrolase activity
GO:0016793 triphosphoric monoester hydrolase activity
GO:0030145 manganese ion binding
GO:0042802 identical protein binding
GO:0050897 cobalt ion binding
Biological Process
GO:0006203 dGTP catabolic process
GO:0015949 nucleobase-containing small molecule interconversion
GO:0043099 pyrimidine deoxyribonucleoside salvage

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:7u67, PDBe:7u67, PDBj:7u67
PDBsum7u67
PubMed36067314
UniProtP15723|DGTP_ECOLI Deoxyguanosinetriphosphate triphosphohydrolase (Gene Name=dgt)

[Back to BioLiP]