Structure of PDB 3fst Chain A

Receptor sequence
>3fstA (length=286) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
FFHASQRDALNQSLAEVQGQINVSFEFFPPRTSEMEQTLWNSIDRLSSLK
PKFVSVTYGANSGERDRTHSIIKGIKDRTGLEAAPHLTCIDATPDELRTI
ARDYWNNGIRHIVALRGDLPEMYASDLVTLLKEVADFDISVAAYPEVHPE
AKSAQADLLNLKRKVDAGANRAITQFFFDVESYLRFRDRCVSAGIDVEII
PGILPVSNFKQAKKLADMTNVRIPAWMAQMFDGLDDDAETRKLVGANIAM
DMVKILSREGVKDFHFYTLNRAEMSYAICHTLGVRP
3D structure
PDB3fst Functional role for the conformationally mobile phenylalanine 223 in the reaction of methylenetetrahydrofolate reductase from Escherichia coli.
ChainA
Resolution1.65 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 E28 D120 L223 H273
Catalytic site (residue number reindexed from 1) S24 E26 D118 L215 H265
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 T59 Y60 A62 H88 L117 R118 G119 D120 Y131 A132 A150 Y152 H156 A159 D165 N168 K172 Q183 T57 Y58 A60 H86 L115 R116 G117 D118 Y123 A124 A142 Y144 H148 A151 D157 N160 K164 Q175
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:3fst, PDBe:3fst, PDBj:3fst
PDBsum3fst
PubMed19610625
UniProtP0AEZ1|METF_ECOLI 5,10-methylenetetrahydrofolate reductase (Gene Name=metF)

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