Structure of PDB 4km0 Chain A

Receptor sequence

>4km0A (length=161) Species: 1773 (Mycobacterium tuberculosis)

SHMVGLIWAQATSGVIGRGGDIPWRLPEDQAHFREITMGHTIVMGRRTWD
SLPAKVRPLPGRRNVVLSRQADFMASGAEVVGSLEEALTSPETWVIGGGQ
VYALALPYATRCEVTEVDIGLPREAGDALAPVLDETWRGETGEWRFSRSG
LRYRLYSYHRS

3D structure

• PDB: 4km0 Mycobacterium tuberculosis Dihydrofolate Reductase Reveals Two Conformational States and a Possible Low Affinity Mechanism to Antifolate Drugs.
• Chain: A
• Resolution: 1.3 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): 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	CP6	A	I5 W6 D27 F31 L50 I94	I7 W8 D29 F33 L52 I96	MOAD: Kd=0.91uM PDBbind-CN: -logKd/Ki=6.04,Kd=0.91uM
BS02	ATR	A	G43 R44 R45 T46 L65 S66 R67 G96 G97 Q98 V99 L102	G45 R46 R47 T48 L67 S68 R69 G98 G99 Q100 V101 L104

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:4km0, PDBe:4km0, PDBj:4km0
• PDBsum: 4km0
• PubMed: 24210757
• UniProt: P9WNX1|DYR_MYCTU Dihydrofolate reductase (Gene Name=folA)