Structure of PDB 3fsu Chain C

Receptor sequence
>3fsuC (length=266) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
QINVSFQFFPPRTSEMEQTLWNSIDRLSSLKPKFVSVTYGANSGERDRTH
SIIKGIKDRTGLEAAPHLTCIDATPDELRTIARDYWNNGIRHIVALRGDL
EMYASDLVTLLKEVADFDISVAAYPEVHPEAKSAQADLLNLKRKVDAGAN
RAITQFFFDVESYLRFRDRCVSAGIDVEIIPGILPVSNFKQAKKLADMTN
VRIPAWMAQMFDGLDDDAETRKLVGANIAMDMVKILSREGVKDFHFYTLN
RAEMSYAICHTLGVRP
3D structure
PDB3fsu Functional role for the conformationally mobile phenylalanine 223 in the reaction of methylenetetrahydrofolate reductase from Escherichia coli.
ChainC
Resolution1.7 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S26 Q28 D120 L223 H273
Catalytic site (residue number reindexed from 1) S5 Q7 D99 L195 H245
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 C T59 Y60 H88 L117 R118 G119 D120 Y131 A132 A150 Y152 H156 A159 D165 N168 R171 K172 T38 Y39 H67 L96 R97 G98 D99 Y103 A104 A122 Y124 H128 A131 D137 N140 R143 K144
BS02 MRY C Q183 F184 Q155 F156
Gene Ontology
Molecular Function
GO:0004489 methylenetetrahydrofolate reductase (NAD(P)H) activity
GO:0016491 oxidoreductase activity
GO:0051087 protein-folding chaperone binding
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
GO:0032991 protein-containing complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3fsu, PDBe:3fsu, PDBj:3fsu
PDBsum3fsu
PubMed19610625
UniProtP0AEZ1|METF_ECOLI 5,10-methylenetetrahydrofolate reductase (Gene Name=metF)

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