Structure of PDB 1zp3 Chain C

Receptor sequence
>1zp3C (length=267) Species: 562 (Escherichia coli) [Search protein sequence]
GQINVSFEFFPPRTSEMEQTLWNSIDRLSSLKPKFVSVTYGANSGERDRT
HSIIKGIKDRTGLEAAPHLTCIDATPDELRTIARDYWNNGIRHIVALRGD
LEMYASDLVTLLKEVADFDISVAAYPEVHPEAKSAQADLLNLKRKVDAGA
NRAITQFFFDVESYLRFRDRCVSAGIDVEIIPGILPVSNFKQAKKFADMT
NVRIPAWMAQMFDGLDDDAETRKLVGANIAMDMVKILSREGVKDFHFYTL
NRAEMSYAICHTLGVRP
3D structure
PDB1zp3 Structures of NADH and CH(3)-H(4)Folate Complexes of Escherichia coli Methylenetetrahydrofolate Reductase Reveal a Spartan Strategy for a Ping-Pong Reaction
ChainC
Resolution1.85 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 F223 H273
Catalytic site (residue number reindexed from 1) S6 E8 D100 F196 H246
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 I181 Q183 T39 Y40 H68 L97 R98 G99 D100 Y104 A105 A123 Y125 H129 A132 D138 N141 R144 K145 I154 Q156
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:1zp3, PDBe:1zp3, PDBj:1zp3
PDBsum1zp3
PubMed16114881
UniProtP0AEZ1|METF_ECOLI 5,10-methylenetetrahydrofolate reductase (Gene Name=metF)

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