Structure of PDB 2dqb Chain F Binding Site BS01

Receptor Information

>2dqb Chain F (length=362) Species: 300852 (Thermus thermophilus HB8)

MRFSREALLELEASRLAPYAQKARDTRGRAHPEPSLYRTPYQKDRDRILH
TTAFRRLEYKTQVLPDYYRTRLTHTLEVAQVSRSIARALGLNEDLTEAIA
LSHDLGHPPFHTGEHVLNALMQDHGGFEHNAQALRILTHLEVRYPGFRGL
NLTYEVLEGIATHEALYEGQGTLEAQVVDLSDAIAYAAHDLDDGFRAGLL
HPEELKEVELLQALALEEGLDLLRLPELDRRVLVRQLLGYFITAAIEATH
RRVEEAGVQSAEAVRRHPSRLAALGEEAEKALKALKAFLMERFYRHPEVL
RERRKAEAVLEGLFAAYTRYPELLPREVQAKIPEEGLERAVCDYIAGMTD
RFALEAYRRLSP

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 2dqb Chain F Residue 505

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2dqb Structure of dNTP-inducible dNTP triphosphohydrolase: insight into broad specificity for dNTPs and triphosphohydrolase-type hydrolysis
• Resolution: 2.2 Å
• Binding residue (original residue number in PDB): H108 H169 E170
• Binding residue (residue number reindexed from 1): H103 H163 E164
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): H79 H108 D109 D196
• Catalytic site (residue number reindexed from 1): H74 H103 D104 D182
• Enzyme Commision number: 3.1.5.1: dGTPase.

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

External links

• PDB: RCSB:2dqb, PDBe:2dqb, PDBj:2dqb
• PDBsum: 2dqb
• PubMed: 17242516
• UniProt: Q5SL81