Structure of PDB 3apy Chain F

Receptor sequence
>3apyF (length=291) Species: 300852 (Thermus thermophilus HB8) [Search protein sequence]
MKIRDLLKARRGPLFSFEFFPPKDPEGEEALFRTLEELKAFRPAFVSITY
GAMGSTRERSVAWAQRIQSLGLNPLAHLTVAGQSRKEVAEVLHRFVESGV
ENLLALRGDPPRGERVFRPHPEGFRYAAELVALIRERYGDRVSVGGAAYP
EGHPESESLEADLRHFKAKVEAGLDFAITQLFFNNAHYFGFLERARRAGI
GIPILPGIMPVTSYRQLRRFTEVCGASIPGPLLAKLERHQDDPKAVLEIG
VEHAVRQVAELLEAGVEGVHFYTLNKSPATRMVLERLGLRP
3D structure
PDB3apy Properties and Crystal Structure of Methylenetetrahydrofolate Reductase from Thermus thermophilus HB8.
ChainF
Resolution2.8 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 F Y50 H77 T79 L106 R107 G108 D109 Y126 A127 A147 Y149 H153 S156 H165 K169 Y50 H77 T79 L106 R107 G108 D109 Y126 A127 A147 Y149 H153 S156 H165 K169
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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Biological Process

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Cellular Component
External links
PDB RCSB:3apy, PDBe:3apy, PDBj:3apy
PDBsum3apy
PubMed21858212
UniProtQ5SLG6

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