Structure of PDB 3fre Chain X

Receptor sequence
>3freX (length=157) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
TLSILVAHDLQRVIGFENQLPWHLPNDLKHVKKLSTGHTLVMGRKTFESI
GKPLPNRRNVVLTSDTSFNVEGVDVIHSIEDIYQLPGHVFIFGGQTLFEE
MIDKVDDMYITVIEGKFRGDTFFPPYTFEDWEVASSVEGKLDEKNTIPHT
FLHLIRK
3D structure
PDB3fre Increased hydrophobic interactions of iclaprim with Staphylococcus aureus dihydrofolate reductase are responsible for the increase in affinity and antibacterial activity
ChainX
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L5
Catalytic site (residue number reindexed from 1) L5
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 X V6 A7 I14 N18 Q19 G43 R44 K45 T46 L62 T63 S64 F92 G94 Q95 T96 E100 T121 V6 A7 I14 N18 Q19 G43 R44 K45 T46 L62 T63 S64 F92 G94 Q95 T96 E100 T121
BS02 TOP X L5 V6 A7 D27 L28 V31 F92 L5 V6 A7 D27 L28 V31 F92 MOAD: Ki=0.0006uM
BindingDB: Ki=3.4nM,IC50=14.4nM
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: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:3fre, PDBe:3fre, PDBj:3fre
PDBsum3fre
PubMed19211577
UniProtP0A017|DYR_STAAU Dihydrofolate reductase (Gene Name=folA)

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