Structure of PDB 1b5t Chain B

Receptor sequence
>1b5tB (length=274) Species: 562 (Escherichia coli) [Search protein sequence]
QINVSFEFFPPRTSEMEQTLWNSIDRLSSLKPKFVSVTYGANSGERDRTH
SIIKGIKDRTGLEAAPHLTCIDATPDELRTIARDYWNNGIRHIVALRGDL
PPGSGKPEMYASDLVTLLKEVADFDISVAAYPEVHPEAKSAQADLLNLKR
KVDAGANRAITQFFFDVESYLRFRDRCVSAGIDVEIIPGILPVSNFKQAK
KFADMTNVRIPAWMAQMFDGLDDDAETRKLVGANIAMDMVKILSREGVKD
FHFYTLNRAEMSYAICHTLGVRPA
3D structure
PDB1b5t The structure and properties of methylenetetrahydrofolate reductase from Escherichia coli suggest how folate ameliorates human hyperhomocysteinemia.
ChainB
Resolution2.5 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) S5 E7 D99 F202 H252
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 Y60 H88 L117 R118 G119 D120 Y131 A132 A150 Y152 H156 A159 D165 N168 K172 Y39 H67 L96 R97 G98 D99 Y110 A111 A129 Y131 H135 A138 D144 N147 K151
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:1b5t, PDBe:1b5t, PDBj:1b5t
PDBsum1b5t
PubMed10201405
UniProtP0AEZ1|METF_ECOLI 5,10-methylenetetrahydrofolate reductase (Gene Name=metF)

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