Structure of PDB 7reg Chain B

Receptor sequence
>7regB (length=157) Species: 562 (Escherichia coli) [Search protein sequence]
MKLSLMVAISKNGVIGNGPDIPWSAKGEQLLFKAITYNQWLLVGRKTFES
MGALPNRKYAVVTRSSFTSDNENVLIFPSIKDALTNLKKITDHVIVSGGG
EIYKSLIDQVDTLHISTIDIEPEGDVYFPEIPSNFRPVFTQDFASNINYS
YQIWQKG
3D structure
PDB7reg Structure-guided functional studies of plasmid-encoded dihydrofolate reductases reveal a common mechanism of trimethoprim resistance in Gram-negative pathogens.
ChainB
Resolution1.77 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 4SI B M6 V7 A8 E28 Q29 F32 K33 M51 L54 M6 V7 A8 E28 Q29 F32 K33 M51 L54
BS02 NAP B V7 A8 I15 G18 P19 D20 I21 G44 R45 K46 T47 V62 T63 R64 P78 S97 G99 G100 E101 I102 V7 A8 I15 G18 P19 D20 I21 G44 R45 K46 T47 V62 T63 R64 P78 S97 G99 G100 E101 I102
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

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Molecular Function
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Biological Process
External links
PDB RCSB:7reg, PDBe:7reg, PDBj:7reg
PDBsum7reg
PubMed35562546
UniProtP00382|DYR1_ECOLX Dihydrofolate reductase type 1 (Gene Name=dhfrI)

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