Structure of PDB 1zp3 Chain A

Receptor sequence
>1zp3A (length=284) Species: 562 (Escherichia coli) [Search protein sequence]
FHASQRDALNQSLAEVQGQINVSFEFFPPRTSEMEQTLWNSIDRLSSLKP
KFVSVTYGANSGERDRTHSIIKGIKDRTGLEAAPHLTCIDATPDELRTIA
RDYWNNGIRHIVALRGDLPMYASDLVTLLKEVADFDISVAAYPEVHPEAK
SAQADLLNLKRKVDAGANRAITQFFFDVESYLRFRDRCVSAGIDVEIIPG
ILPVSNFKQAKKFADMTNVRIPAWMAQMFDGLDDDAETRKLVGANIAMDM
VKILSREGVKDFHFYTLNRAEMSYAICHTLGVRP
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
ChainA
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) S23 E25 D117 F213 H263
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 T90 L117 R118 G119 D120 Y131 A132 A150 Y152 H156 E158 A159 D165 N168 R171 K172 I181 T56 Y57 A59 H85 T87 L114 R115 G116 D117 Y121 A122 A140 Y142 H146 E148 A149 D155 N158 R161 K162 I171
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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