Structure of PDB 5ujf Chain A

Receptor sequence
>5ujfA (length=161) Species: 83332 (Mycobacterium tuberculosis H37Rv) [Search protein sequence]
HMMVGLIWAQATSGVIGRGGDIPWRLPEDQAHFREITMGHTIVMGRRTWD
SLPAKVRPLPGRRNVVLSRQADFMASGAEVVGSLEEALTSPETWVIGGGQ
VYALALPYATRCEVTEVDIGLPREAGDALAPVLDETWRGETGEWRFSRSG
LRYRLYSYHRS
3D structure
PDB5ujf Crystal Structure of Mycobacterium tuberculosis Dihydrofolate Reductase Bound p218 Inhibitor
ChainA
Resolution2.3 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) I5 I20 W22 D27 Q28 F31 L57 T91 T113
Catalytic site (residue number reindexed from 1) I7 I22 W24 D29 Q30 F33 L59 T93 T115
Enzyme Commision number 1.5.1.3: dihydrofolate reductase.
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 MMV A I5 W6 G17 D27 Q28 F31 R32 P51 R60 I94 I7 W8 G19 D29 Q30 F33 R34 P53 R62 I96
Gene Ontology
Molecular Function
GO:0004146 dihydrofolate reductase activity
GO:0016491 oxidoreductase activity
GO:0050661 NADP binding
GO:0070401 NADP+ binding
Biological Process
GO:0006730 one-carbon metabolic process
GO:0046452 dihydrofolate metabolic process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046655 folic acid metabolic process
Cellular Component
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:5ujf, PDBe:5ujf, PDBj:5ujf
PDBsum5ujf
PubMed
UniProtP9WNX1|DYR_MYCTU Dihydrofolate reductase (Gene Name=folA)

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