Structure of PDB 2dqb Chain F

Receptor sequence
>2dqbF (length=362) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
MRFSREALLELEASRLAPYAQKARDTRGRAHPEPSLYRTPYQKDRDRILH
TTAFRRLEYKTQVLPDYYRTRLTHTLEVAQVSRSIARALGLNEDLTEAIA
LSHDLGHPPFHTGEHVLNALMQDHGGFEHNAQALRILTHLEVRYPGFRGL
NLTYEVLEGIATHEALYEGQGTLEAQVVDLSDAIAYAAHDLDDGFRAGLL
HPEELKEVELLQALALEEGLDLLRLPELDRRVLVRQLLGYFITAAIEATH
RRVEEAGVQSAEAVRRHPSRLAALGEEAEKALKALKAFLMERFYRHPEVL
RERRKAEAVLEGLFAAYTRYPELLPREVQAKIPEEGLERAVCDYIAGMTD
RFALEAYRRLSP
3D structure
PDB2dqb Structure of dNTP-inducible dNTP triphosphohydrolase: insight into broad specificity for dNTPs and triphosphohydrolase-type hydrolysis
ChainF
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
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 MG F H108 H169 E170 H103 H163 E164
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:2dqb, PDBe:2dqb, PDBj:2dqb
PDBsum2dqb
PubMed17242516
UniProtQ5SL81

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