Structure of PDB 7rgj Chain A

Receptor sequence
>7rgjA (length=154) Species: 562 (Escherichia coli) [Search protein sequence]
MKLSLMVAISKNGVIGNGPDIPWSAKGEQLLFKAITYNQWLLVGRKTFES
MGALPNRKYAVVTRSFTSNENVLIFPSIKDALTNLKKITDHVIVSGGGEI
YKSLIDQVDTLHISTIDIEPEGDVYFPEIPSNFRPVFTQDFASNINYSYQ
IWQK
3D structure
PDB7rgj Structure-guided functional studies of plasmid-encoded dihydrofolate reductases reveal a common mechanism of trimethoprim resistance in Gram-negative pathogens.
ChainA
Resolution1.44 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 NAP A V7 A8 I15 G18 D20 I21 G44 R45 K46 T47 V62 T63 R64 G99 G100 E101 I102 V7 A8 I15 G18 D20 I21 G44 R45 K46 T47 V62 T63 R64 G97 G98 E99 I100
BS02 8MU A M6 V7 A8 I21 W23 E28 F32 M51 M6 V7 A8 I21 W23 E28 F32 M51
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
View graph for
Biological Process
External links
PDB RCSB:7rgj, PDBe:7rgj, PDBj:7rgj
PDBsum7rgj
PubMed35562546
UniProtP00382|DYR1_ECOLX Dihydrofolate reductase type 1 (Gene Name=dhfrI)

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