Structure of PDB 7myl Chain E

Receptor sequence
>7mylE (length=156) Species: 573 (Klebsiella pneumoniae) [Search protein sequence]
MKLSLMVAISKNGVIGNGPDIPWSAKGEQLLFKAITYNQWLLVGRKTFES
MGALPNRKYAVVTRSSFTSDNENVLIFPSIKDALTNLKKITDHVIVSGGG
EIYKSLIDQVDTLHISTIDIEPEGDVYFPEIPSNFRPVFTQDFASNINYS
YQIWQK
3D structure
PDB7myl Structure-guided functional studies of plasmid-encoded dihydrofolate reductases reveal a common mechanism of trimethoprim resistance in Gram-negative pathogens.
ChainE
Resolution2.15 Å
3D
structure
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Enzymatic activity
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 M6 V7 A8 N17 F32 S50 M51 S97 M6 V7 A8 N17 F32 S50 M51 S97
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004146 dihydrofolate reductase activity
GO:0016491 oxidoreductase activity
GO:0050661 NADP binding
Biological Process
GO:0046452 dihydrofolate metabolic process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046655 folic acid metabolic process

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Molecular Function
View graph for
Biological Process
External links
PDB RCSB:7myl, PDBe:7myl, PDBj:7myl
PDBsum7myl
PubMed35562546
UniProtA4GRC7

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