Structure of PDB 2w9s Chain E

Receptor sequence
>2w9sE (length=157) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
TLSIIVAHDKQRVIGYQNQLPWHLPNDLKHIKQLTTGNTLVMARKTFESI
GKPLPNRRNVVLTNQASFHHEGVDVINSLDEIKELSGHVFIFGGQTLYEA
MIDQVDDMYITVIDGKFQGDTFFPPYTFEDWEVESSVEGQLDEKNTIPHT
FLHLVRR
3D structure
PDB2w9s Structural Comparison of Chromosomal and Exogenous Dihydrofolate Reductase from Staphylococcus Aureus in Complex with the Potent Inhibitor Trimethoprim.
ChainE
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) I5 L20 W22 D27 L28 I31 L54 V89 T111
Catalytic site (residue number reindexed from 1) I5 L20 W22 D27 L28 I31 L54 V89 T111
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 TOP E I5 V6 A7 L20 D27 I31 F92 I5 V6 A7 L20 D27 I31 F92 MOAD: Kd=730nM
BindingDB: IC50=1.51e+4nM
Gene Ontology
Molecular Function
GO:0004146 dihydrofolate reductase activity
GO:0016491 oxidoreductase activity
GO:0050661 NADP binding
Biological Process
GO:0006730 one-carbon metabolic process
GO:0031427 response to methotrexate
GO:0046452 dihydrofolate metabolic process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046655 folic acid metabolic process
GO:0046677 response to antibiotic
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:2w9s, PDBe:2w9s, PDBj:2w9s
PDBsum2w9s
PubMed19280600
UniProtP13955|DYRA_STAAU Dihydrofolate reductase type 1 from Tn4003 (Gene Name=dfrA)

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