Structure of PDB 3jw3 Chain A

Receptor sequence
>3jw3A (length=165) Species: 1392 (Bacillus anthracis) [Search protein sequence]
HHHMRVSFMVAMDENRVIGKDNNLPWRLPSELQYVKKTTMGHPLIMGRKN
YEAIGRPLPGRRNIIVTRNEGYHVEGCEVAHSVEEVFELCKNEEEIFIIG
GAQIYDLFLPYVDKLYITKIHHAFEGDTFFPEMDMTNWKEVFVEKGLTDE
KNPYTYYYHVYEKQQ
3D structure
PDB3jw3 Mutational Studies into Trimethoprim Resistance in Bacillus anthracis Dihydrofolate Reductase
ChainA
Resolution2.57 Å
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) M9 L24 W26 E31 L32 V35 L58 I96 T118
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 V7 A8 I15 N19 N20 L21 G44 R45 K46 N47 V63 T64 R65 H78 I96 G97 G98 A99 Q100 I101 L104 V10 A11 I18 N22 N23 L24 G47 R48 K49 N50 V66 T67 R68 H81 I99 G100 G101 A102 Q103 I104 L107
BS02 TOP A M6 V7 A8 E28 V32 I51 I96 M9 V10 A11 E31 V35 I54 I99 BindingDB: Ki=24100nM,IC50=71000nM
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:3jw3, PDBe:3jw3, PDBj:3jw3
PDBsum3jw3
PubMed
UniProtQ81R22

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