Structure of PDB 7km8 Chain A

Receptor sequence

>7km8A (length=158) Species: 362242 (Mycobacterium ulcerans Agy99)

TSVGLIWAQSTSGVIGRDGGIPWRLPEDLAHFKRLTMGHTVVMGRRTWDS
LPAAHRPLPGRRNVVVTRQTGLVAHGAQVVGSLEQALSATWVIGGAQIYA
LALPLANRCEVTEVDVDLPPEDEDALAPVLDQTWAGTSGEWLVSRSGLRY
RMHSYRRL

3D structure

• PDB: 7km8 Crystal Structure of Dihydrofolate reductase (DHFR) from Mycobacterium ulcerans Agy99 in complex with NADP and inhibitor SDDC-0001914, orthorhombic crystal form
• Chain: A
• Resolution: 1.55 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): I7 I22 W24 D29 L30 F33 L59 T97 T119
• Catalytic site (residue number reindexed from 1): I6 I21 W23 D28 L29 F32 L58 T90 T112
• 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	NAP	A	W8 A9 I16 G17 G21 I22 G45 R46 R47 T48 S51 V67 T68 R69 Q70 I100 G102 A103 Q104 I105 L108 A132	W7 A8 I15 G16 G20 I21 G44 R45 R46 T47 S50 V66 T67 R68 Q69 I93 G95 A96 Q97 I98 L101 A125
BS02	WPD	A	I7 W8 D29 L30 F33 L52 P53 H56 L59 R62 I100	I6 W7 D28 L29 F32 L51 P52 H55 L58 R61 I93
BS03	WPD	A	R25 S153	R24 S146

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0004146 dihydrofolate reductase activity
• GO:0016491 oxidoreductase activity
• GO:0050661 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:7km8, PDBe:7km8, PDBj:7km8
• PDBsum: 7km8
• UniProt: A0PQG8