Structure of PDB 5a64 Chain A

Receptor sequence
>5a64A (length=203) Species: 10090 (Mus musculus) [Search protein sequence]
GLIEVERKFAPGPDTEERLQELGATLEHRVTFRDTYYDTSELSLMLSDHW
LRQREGSGWELKCPGVTGVSGPHNEYVEVTSEAAIVAQLFELLGSGEQKP
AGVAAVLGSLKLQEVASFITTRSSWKLAQLTIDLDSADFGYAVGEVEAMV
HEKAEVPAALEKIITVSSMLGVPAQEEAPAKLMVYLQRFRPLDYQRLLEA
ASS
3D structure
PDB5a64 Structural Determinants for Substrate Binding and Catalysis in Triphosphate Tunnel Metalloenzymes.
ChainA
Resolution2.1 Å
3D
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Enzymatic activity
Enzyme Commision number 3.6.1.28: thiamine-triphosphatase.
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 V4E A K11 Y39 W53 R55 R57 K65 Y79 R125 E157 K193 K8 Y36 W50 R52 R54 K62 Y76 R122 E145 K181
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0016462 pyrophosphatase activity
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
GO:0050333 thiamine triphosphate phosphatase activity
Biological Process
GO:0006772 thiamine metabolic process
GO:0009229 thiamine diphosphate biosynthetic process
GO:0016311 dephosphorylation
GO:0042357 thiamine diphosphate metabolic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:5a64, PDBe:5a64, PDBj:5a64
PDBsum5a64
PubMed26221030
UniProtQ8JZL3|THTPA_MOUSE Thiamine-triphosphatase (Gene Name=Thtpa)

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