Structure of PDB 6nne Chain A

Receptor sequence
>6nneA (length=159) Species: 419947 (Mycobacterium tuberculosis H37Ra) [Search protein sequence]
MVGLIWAQATSGVIGRGGDIPWRLPEDQAHFREITMGHTIVMGRRTWDSL
PAKVRPLPGRRNVVLSRQADFMASGAEVVGSLEEALTSPETWVIGGGQVY
ALALPYATRCEVTEVDIGLPREAGDALAPVLDETWRGETGEWRFSRSGLR
YRLYSYHRS
3D structure
PDB6nne Crystal structures of the closed form of Mycobacterium tuberculosis dihydrofolate reductase in complex with dihydrofolate and antifolates.
ChainA
Resolution1.595 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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 NDP A W6 A7 I14 G18 D19 I20 G43 R44 R45 T46 L65 S66 R67 I94 G96 G97 Q98 V99 W6 A7 I14 G18 D19 I20 G43 R44 R45 T46 L65 S66 R67 I94 G96 G97 Q98 V99
BS02 KUP A I5 W6 I20 R23 D27 Q28 F31 L50 I94 I5 W6 I20 R23 D27 Q28 F31 L50 I94 MOAD: Kd=2.2uM
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:6nne, PDBe:6nne, PDBj:6nne
PDBsum6nne
PubMed31282477
UniProtA5U6B6

[Back to BioLiP]