Structure of PDB 3p2o Chain B

Receptor sequence
>3p2oB (length=282) Species: 192222 (Campylobacter jejuni subsp. jejuni NCTC 11168 = ATCC 700819) [Search protein sequence]
AMTLLDGKALSAKIKEELKEKNQFLKSKGIESCLAVILVGDNPASQTYVK
SKAKACEECGIKSLVYHLNENITQNELLALINTLNHDDSVHGILVQLPLP
DHICKDLILESIISSKDVDGFHPINVGYLNLGLESGFLPCTPLGVMKLLK
AYEIDLEGKDAVIIGASNIVGRPMATMLLNAGATVSVCHIKTKDLSLYTR
QADLIIVAAGCVNLLRSDMVKEGVIVVDVGINRLESGKIVGDVDFEEVSK
KSSYITPVPGGVGPMTIAMLLENTVKSAKNRL
3D structure
PDB3p2o Crystal Structure of FolD Bifunctional Protein from
ChainB
Resolution2.227 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) S44 K51 Q95 D118
Catalytic site (residue number reindexed from 1) S45 K52 Q96 D119
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 NAD B Y47 G164 A165 S166 V169 H188 I189 A207 A208 L213 V228 I230 Y48 G165 A166 S167 V170 H189 I190 A208 A209 L214 V229 I231
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
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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Cellular Component
External links
PDB RCSB:3p2o, PDBe:3p2o, PDBj:3p2o
PDBsum3p2o
PubMed
UniProtQ0PA35|FOLD_CAMJE Bifunctional protein FolD (Gene Name=folD)

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