Structure of PDB 4km2 Chain A

Receptor sequence

>4km2A (length=159) Species: 1773 (Mycobacterium tuberculosis)

MVGLIWAQATSGVIGRGGDIPWRLPEDQAHFREITMGHTIVMGRRTWDSL
PAKVRPLPGRRNVVLSRQADFMASGAEVVGSLEEALTSPETWVIGGGQVY
ALALPYATRCEVTEVDIGLPREAGDALAPVLDETWRGETGEWRFSRSGLR
YRLYSYHRS

3D structure

• PDB: 4km2 Mycobacterium tuberculosis Dihydrofolate Reductase Reveals Two Conformational States and a Possible Low Affinity Mechanism to Antifolate Drugs.
• Chain: A
• Resolution: 1.4 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): I5 I20 W22 D27 Q28 F31 L57 T91 T113
• 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	ATR	A	G43 R44 R45 T46 L65 S66 R67 Q68 G80 G96 Q98 V99 L102	G43 R44 R45 T46 L65 S66 R67 Q68 G80 G96 Q98 V99 L102
BS02	TOP	A	I5 W6 D27 F31 I94	I5 W6 D27 F31 I94	MOAD: Kd=1.43uM PDBbind-CN: -logKd/Ki=5.84,Kd=1.43uM BindingDB: IC50=88000nM

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:4km2, PDBe:4km2, PDBj:4km2
• PDBsum: 4km2
• PubMed: 24210757
• UniProt: P9WNX1|DYR_MYCTU Dihydrofolate reductase (Gene Name=folA)