Structure of PDB 6pey Chain B

Receptor sequence
>6peyB (length=290) Species: 562 (Escherichia coli) [Search protein sequence]
FFHASQRDALNQSLAEVQGQINVSFEFFPPRTSEMEQTLWNSIDRLSSLK
PKFVSVTYGANSGERDRTHSIIKGIKDRTGLEAAPHLTCIDATPDELRTI
ARDYWNNGIRHIVALRGALPPGKPEMYASDLVTLLKEVADFDISVAAYPE
VHPEAKSAQADLLNLKRKVDAGANRAITQFFFDVESYLRFRDRCVSAGID
VEIIPGILPVSNFKQAKKFADMTNVRIPAWMAQMFDGLDDDAETRKLVGA
NIAMDMVKILSREGVKDFHFYTLNRAEMSYAICHTLGVRP
3D structure
PDB6pey Examination of Asp120Ala a Chemically Important Novel Mutation in the Enzyme Mthylenetetrahydrofolate Reductase
ChainB
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) S24 E26 A118 F219 H269
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 B T59 Y60 H88 L117 R118 G119 Y131 A132 A150 Y152 H156 A159 D165 N168 R171 K172 Q183 T57 Y58 H86 L115 R116 G117 Y127 A128 A146 Y148 H152 A155 D161 N164 R167 K168 Q179
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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