Structure of PDB 4elg Chain A

Receptor sequence
>4elgA (length=166) Species: 260799 (Bacillus anthracis str. Sterne) [Search protein sequence]
MIVSFMVAMDENRVIGKDNNLPWRLPSELQYVKKTTMGHPLIMGRKNYEA
IGRPLPGRRNIIVTRNEGYHVEGCEVAHSVEEVFELCKNEEEIFIFGGAQ
IYDLFLPYVDKLYITKIHHAFEGDTFFPEMDMTNWKEVFVEKGLTDEKNP
YTYYYHVYEKQQLVPR
3D structure
PDB4elg Structure-activity relationship for enantiomers of potent inhibitors of B. anthracis dihydrofolate reductase.
ChainA
Resolution2.101 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) 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 52J A M6 V7 A8 N20 L21 E28 L29 Q30 V32 K33 I51 L55 P56 R58 F96 M6 V7 A8 N20 L21 E28 L29 Q30 V32 K33 I51 L55 P56 R58 F96 MOAD: Ki=6.9nM
PDBbind-CN: -logKd/Ki=8.16,Ki=6.9nM
BS02 CA A Y108 D110 Y108 D110
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:4elg, PDBe:4elg, PDBj:4elg
PDBsum4elg
PubMed22999981
UniProtQ81R22

[Back to BioLiP]