Structure of PDB 2kgk Chain A

Receptor sequence
>2kgkA (length=162) Species: 1392 (Bacillus anthracis) [Search protein sequence]
MIVSFMVAMDENRVIGKDNNLPWRLPSELQYVKKTTMGHPLIMGRKNYEA
IGRPLPGRRNIIVTRNEGYHVEGCEVAHSVEEVFELCKNEEEIFIFGGAQ
IYDLFLPYVDKLYITKIHHAFEGDTFFPEMDMTNWKEVFVEKGLTDEKNP
YTYYYHVYEKQQ
3D structure
PDB2kgk The solution structure of Bacillus anthracis dihydrofolate reductase yields insight into the analysis of structure-activity relationships for novel inhibitors.
ChainA
ResolutionN/A
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) M6 L21 W23 E28 L29 V32 L55 I93 T115
Catalytic site (residue number reindexed from 1) M6 L21 W23 E28 L29 V32 L55 I93 T115
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 A8 I15 N19 L21 R45 K46 N47 T64 R65 S79 F96 G98 A99 Q100 I101 A8 I15 N19 L21 R45 K46 N47 T64 R65 S79 F96 G98 A99 Q100 I101
BS02 N22 A L21 W23 I51 R53 L21 W23 I51 R53 BindingDB: IC50=890nM,Ki=300nM
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

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Cellular Component
External links
PDB RCSB:2kgk, PDBe:2kgk, PDBj:2kgk
PDBsum2kgk
PubMed19323450
UniProtQ81R22

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