Structure of PDB 7km9 Chain A

Receptor sequence

>7km9A (length=158) Species: 362242 (Mycobacterium ulcerans Agy99)

SVGLIWAQSTSGVIGRDGGIPWRLPEDLAHFKRLTMGHTVVMGRRTWDSL
PAAHRPLPGRRNVVVTRQTGLVAHGAQVVGSLEQALSAATWVIGGAQIYA
LALPLANRCEVTEVDVDLPPEDEDALAPVLDQTWAGTSGEWLVSRSGLRY
RMHSYRRL

3D structure

• PDB: 7km9 Crystal Structure of Dihydrofolate reductase (DHFR) from Mycobacterium ulcerans Agy99 in complex with NADP and inhibitor SDDC-0001913, tetragonal crystal form
• Chain: A
• Resolution: 1.95 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): I5 I20 W22 D27 L28 F31 L57 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 G45 R46 R47 T48 V67 T68 R69 Q70 G82 I100 G101 G102 A103 Q104 I105	W6 A7 I14 G15 G19 G43 R44 R45 T46 V65 T66 R67 Q68 G80 I93 G94 G95 A96 Q97 I98
BS02	WPJ	A	I7 W8 D29 L30 F33 L52 P53 R62 I100	I5 W6 D27 L28 F31 L50 P51 R60 I93

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:7km9, PDBe:7km9, PDBj:7km9
• PDBsum: 7km9
• UniProt: A0PQG8