Structure of PDB 6pey Chain C

Receptor sequence
>6peyC (length=271) Species: 562 (Escherichia coli) [Search protein sequence]
GQINVSFEFFPPRTSEMEQTLWNSIDRLSSLKPKFVSVTYGANSGERDRT
HSIIKGIKDRTGLEAAPHLTCIDATPDELRTIARDYWNNGIRHIVALRGA
LPPGPEMYASDLVTLLKEVADFDISVAAYPEVHPEAKSAQADLLNLKRKV
DAGANRAITQFFFDVESYLRFRDRCVSAGIDVEIIPGILPVSNFKQAKKF
ADMTNVRIPAWMAQMFDGLDDDAETRKLVGANIAMDMVKILSREGVKDFH
FYTLNRAEMSYAICHTLGVRP
3D structure
PDB6pey Examination of Asp120Ala a Chemically Important Novel Mutation in the Enzyme Mthylenetetrahydrofolate Reductase
ChainC
Resolution2.88 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 A120 F223 H273
Catalytic site (residue number reindexed from 1) S6 E8 A100 F200 H250
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 Y131 A150 Y152 H156 A159 N168 K172 I181 Q183 T39 Y40 H68 L97 R98 Y108 A127 Y129 H133 A136 N145 K149 I158 Q160
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:6pey, PDBe:6pey, PDBj:6pey
PDBsum6pey
PubMed
UniProtP0AEZ1|METF_ECOLI 5,10-methylenetetrahydrofolate reductase (Gene Name=metF)

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