Structure of PDB 5u26 Chain A

Receptor sequence

>5u26A (length=166) Species: 1773 (Mycobacterium tuberculosis)

LVPRGSHMVGLIWAQATSGVIGRGGDIPWRLPEDQAHFREITMGHTIVMG
RRTWDSLPAKVRPLPGRRNVVLSRQADFMASGAEVVGSLEEALTSPETWV
IGGGQVYALALPYATRCEVTEVDIGLPREAGDALAPVLDETWRGETGEWR
FSRSGLRYRLYSYHRS

3D structure

• PDB: 5u26 Crystal Structure of Mycobacterium tuberculosis Dihydrofolate Reductase Bound to NADP and p218 Inhibitor
• Chain: A
• Resolution: 1.85 Å

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): I12 I27 W29 D34 Q35 F38 L64 T98 T120
• 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 D27 Q28 F31 R32 L50 L57 R60 I94	I12 W13 D34 Q35 F38 R39 L57 L64 R67 I101
BS02	NAP	A	W6 A7 I14 G15 D19 I20 G43 R44 R45 T46 S49 L65 S66 R67 I94 G96 G97 Q98 V99 A126	W13 A14 I21 G22 D26 I27 G50 R51 R52 T53 S56 L72 S73 R74 I101 G103 G104 Q105 V106 A133

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

External links

• PDB: RCSB:5u26, PDBe:5u26, PDBj:5u26
• PDBsum: 5u26
• UniProt: P9WNX1|DYR_MYCTU Dihydrofolate reductase (Gene Name=folA)