Structure of PDB 5xd5 Chain A

Receptor sequence
>5xd5A (length=289) Species: 246196 (Mycolicibacterium smegmatis MC2 155) [Search protein sequence]
TVRAAGAVLWRDATVEVAVIHRPRYDDWSLPKGKLDQGETEPVAAAREIH
EETGHTAVLGRRLGRVTYPIPQGTKRVWYWAAKSTGGDFSPNDEVDKLVW
LPVDAAMDQLQYPDDRKVLRRFVKRPVDTKTVLVVRHGTAGRRSRYKGDD
RKRPLDKRGRAQAEALVAQLMAFGATTLYAADRVRCHQTIEPLAQELDQL
IHNEPLLTEEAYAADHKAARKRLLEIAGRPGNPVICTQGKVIPGLIEWWC
ERAKVRPETTGNRKGSTWVLSLSDGELVGADYLSPPDEK
3D structure
PDB5xd5 Hydrolysis of diadenosine polyphosphates. Exploration of an additional role of Mycobacterium smegmatis MutT1
ChainA
Resolution1.75 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T23 A29
Catalytic site (residue number reindexed from 1) T1 A7
Enzyme Commision number 3.6.1.58: 8-oxo-dGDP phosphatase.
3.6.1.61: diadenosine hexaphosphate hydrolase (ATP-forming).
3.6.1.69: 8-oxo-(d)GTP phosphatase.
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 ATP A R55 Y58 K65 K67 Y101 K108 Y145 R22 Y25 K32 K34 Y68 K75 Y112
BS02 MG A K65 E85 E127 K32 E52 E94
BS03 MG A E81 E85 E127 E48 E52 E94
Gene Ontology
Molecular Function
GO:0008413 8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity
GO:0016787 hydrolase activity
GO:0044715 8-oxo-dGDP phosphatase activity
GO:0044716 8-oxo-GDP phosphatase activity
GO:0046872 metal ion binding
Biological Process
GO:0006260 DNA replication
GO:0006281 DNA repair

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Molecular Function
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Biological Process
External links
PDB RCSB:5xd5, PDBe:5xd5, PDBj:5xd5
PDBsum5xd5
PubMed28705712
UniProtA0QUZ2|MUTT1_MYCS2 8-oxo-(d)GTP phosphatase (Gene Name=mutT1)

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