Structure of PDB 7k6c Chain F

Receptor sequence

>7k6cF (length=159) Species: 561007 (Mycobacteroides abscessus ATCC 19977)

GTIGLIWAQTRAGVIGADGAIPWRLPEDQARFKRITMGHTVIMGRKTWES
LPGSVRPLPGRPNIVLTRDALFEPDGALAVGSADAALAASDEAPWVIGGG
EIYRLFLPLAQRCEVTVVEADVPGDALAPELGEGWVVETNDWQTSESGLR
YQFLSYRKV

3D structure

• PDB: 7k6c Crystal Structure of Dihydrofolate reductase (DHFR) from Mycobacterium abscessus ATCC 19977 / DSM 44196 with NADP and inhibitor P218
• Chain: F
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): I8 I23 W25 D30 Q31 F34 L60 P96 T118
• Catalytic site (residue number reindexed from 1): I6 I21 W23 D28 Q29 F32 L58 P94 T116
• 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	F	W9 A10 I17 G21 A22 I23 G46 R47 K48 T49 L68 T69 R70 G83 I99 G101 G102 E103 I104	W7 A8 I15 G19 A20 I21 G44 R45 K46 T47 L66 T67 R68 G81 I97 G99 G100 E101 I102
BS02	MMV	F	I8 W9 D30 Q31 F34 L53 L60 R63 I99	I6 W7 D28 Q29 F32 L51 L58 R61 I97

Gene Ontology

Molecular Function

• GO:0000166 nucleotide binding
• GO:0004146 dihydrofolate reductase activity
• GO:0016491 oxidoreductase activity
• GO:0046872 metal ion binding
• 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:7k6c, PDBe:7k6c, PDBj:7k6c
• PDBsum: 7k6c
• UniProt: B1MD46