Structure of PDB 3apt Chain A

Receptor sequence
>3aptA (length=292) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
MKIRDLLKARRGPLFSFEFFPPKDPEGEEALFRTLEELKAFRPAFVSITY
GAMGSTRERSVAWAQRIQSLGLNPLAHLTVAGQSRKEVAEVLHRFVESGV
ENLLALRGDPPRGERVFRPHPEGFRYAAELVALIRERYGDRVSVGGAAYP
EGHPESESLEADLRHFKAKVEAGLDFAITQLFFNNAHYFGFLERARRAGI
GIPILPGIMPVTSYRQLRRFTEVCGASIPGPLLAKLERHQDDPKAVLEIG
VEHAVRQVAELLEAGVEGVHFYTLNKSPATRMVLERLGLRPA
3D structure
PDB3apt Properties and Crystal Structure of Methylenetetrahydrofolate Reductase from Thermus thermophilus HB8.
ChainA
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S16 E18 D109 F220 H270
Catalytic site (residue number reindexed from 1) S16 E18 D109 F220 H270
Enzyme Commision number 1.5.1.54: methylenetetrahydrofolate reductase (NADH).
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 FAD A T49 Y50 H77 L106 R107 G108 D109 Y126 A127 A147 Y149 H153 E155 S156 H165 K169 Q180 Y272 T49 Y50 H77 L106 R107 G108 D109 Y126 A127 A147 Y149 H153 E155 S156 H165 K169 Q180 Y272
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004489 methylenetetrahydrofolate reductase (NAD(P)H) activity
GO:0016491 oxidoreductase activity
GO:0071949 FAD binding
GO:0106312 methylenetetrahydrofolate reductase (NADH) activity
Biological Process
GO:0006555 methionine metabolic process
GO:0009086 methionine biosynthetic process
GO:0035999 tetrahydrofolate interconversion
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:3apt, PDBe:3apt, PDBj:3apt
PDBsum3apt
PubMed21858212
UniProtQ5SLG6

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