Structure of PDB 6pey Chain A

Receptor sequence
>6peyA (length=287) Species: 562 (Escherichia coli) [Search protein sequence]
FHASQRDALNQSLAEVQGQINVSFEFFPPRTSEMEQTLWNSIDRLSSLKP
KFVSVTYGANSGERDRTHSIIKGIKDRTGLEAAPHLTCIDATPDELRTIA
RDYWNNGIRHIVALRGALPPGEMYASDLVTLLKEVADFDISVAAYPEVHP
EAKSAQADLLNLKRKVDAGANRAITQFFFDVESYLRFRDRCVSAGIDVEI
IPGILPVSNFKQAKKFADMTNVRIPAWMAQMFDGLDDDAETRKLVGANIA
MDMVKILSREGVKDFHFYTLNRAEMSYAICHTLGVRP
3D structure
PDB6pey Examination of Asp120Ala a Chemically Important Novel Mutation in the Enzyme Mthylenetetrahydrofolate Reductase
ChainA
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) S23 E25 A117 F216 H266
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 H88 L117 R118 Y131 A150 Y152 H156 A159 N168 K172 T56 H85 L114 R115 Y124 A143 Y145 H149 A152 N161 K165
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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