Structure of PDB 5o22 Chain D

Receptor sequence
>5o22D (length=273) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
GAAKIIDGKTIAQQVRSEVAQKVQARIAAGLRAPGLAVVLVGYVASKRKA
CEEVGFVSRSYDLPETTSEAELLELIDTLNADNTIDGILVQLPLPAGIDN
VKVLERIHPDKDVDGFHPYNVGRLCQRAPRLRPCTPRGIVTLLERYNIDT
FGLNAVVIGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHVENADLLI
VAVGKPGFIPGDWIKEGAIVIDVGINRVVGDVVFEDAAKRASYITPVPGG
VGPMTVATLIENTLQACVEYHDP
3D structure
PDB5o22 The natural product carolacton inhibits folate-dependent C1 metabolism by targeting FolD/MTHFD.
ChainD
Resolution2.1 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.5.1.5: methylenetetrahydrofolate dehydrogenase (NADP(+)).
3.5.4.9: methenyltetrahydrofolate cyclohydrolase.
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 C3R D Y50 K54 P260 G264 P265 V268 Y43 K47 P248 G252 P253 V256 MOAD: Kd=10nM
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004477 methenyltetrahydrofolate cyclohydrolase activity
GO:0004488 methylenetetrahydrofolate dehydrogenase (NADP+) activity
GO:0016491 oxidoreductase activity
GO:0016787 hydrolase activity
GO:0042803 protein homodimerization activity
Biological Process
GO:0000105 L-histidine biosynthetic process
GO:0006164 purine nucleotide biosynthetic process
GO:0006730 one-carbon metabolic process
GO:0009086 methionine biosynthetic process
GO:0035999 tetrahydrofolate interconversion
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Cellular Component
External links
PDB RCSB:5o22, PDBe:5o22, PDBj:5o22
PDBsum5o22
PubMed29142318
UniProtP24186|FOLD_ECOLI Bifunctional protein FolD (Gene Name=folD)

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