Structure of PDB 4x9e Chain B Binding Site BS01

Receptor Information

>4x9e Chain B (length=495) Species: 83333 (Escherichia coli K-12)

AQIDFRKKINWHRRYRSPQGVKTEHEILRIFESDRGRIINSPAIRRLQQK
TQVFPNAAVRTRLTHSMEVQQVGRYIAKEILSRLKELKLLEAYGLDELTG
PFESIVEMSCLMHDIGNPPFGHFGEAAINDWFRQRLHPEDAQPLTDDRCS
VAALRLRDGEEPLNELRRKIRQDLCHFEGNAQGIRLVHTLMRMNLTWAQV
GGILKYTRPAWWRGETPETHHYLMKKPGYYLSEEAYIARLRKELNLALYS
RFPLTWIMEAADDISYCVADLEDAVEKRIFTVEQLYHHLHEAWGQHEKGS
LFSLVVENAWEKSRSRSTEDQFFMYLRVNTLNKLVPYAAQRFIDNLPAIF
AGTFNHALLEDASECSDLLKLYKNVAVKHVFSHPDVERLELQGYRVISGL
LEIYRPLLSLSLSDFTELVEKERVKRFPIESRLFHKLSTRHRLAYVEAVS
KLPSDSPEFPLWEYYYRCRLLQDYISGMTDLYAWDEYRRLMAVEQ

Ligand information

>4x9e Chain G (length=3)

ccc

...

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4x9e Structure of Escherichia coli dGTP Triphosphohydrolase: A HEXAMERIC ENZYME WITH DNA EFFECTOR MOLECULES.
• Resolution: 3.1 Å
• Binding residue (original residue number in PDB): Y79 M334 R337 V338
• Binding residue (residue number reindexed from 1): Y75 M324 R327 V328

Enzymatic activity

• Catalytic site (original residue number in PDB): H69 H117 D118 D268 R442
• Catalytic site (residue number reindexed from 1): H65 H113 D114 D262 R432
• Enzyme Commision number: 3.1.5.1: dGTPase.

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

External links

• PDB: RCSB:4x9e, PDBe:4x9e, PDBj:4x9e
• PDBsum: 4x9e
• PubMed: 25694425
• UniProt: P15723|DGTP_ECOLI Deoxyguanosinetriphosphate triphosphohydrolase (Gene Name=dgt)