Structure of PDB 7mym Chain C

Receptor sequence
>7mymC (length=158) Species: 562 (Escherichia coli) [Search protein sequence]
MISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESI
GRPLPGRKNIILSSQPGTDDRVTWVKSVDEAIAACGDVPEIMVIGGGRVY
EQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHS
YCFEILER
3D structure
PDB7mym Structure-guided functional studies of plasmid-encoded dihydrofolate reductases reveal a common mechanism of trimethoprim resistance in Gram-negative pathogens.
ChainC
Resolution3.04 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 ARG C D131 D132 W133 R158 D131 D132 W133 R158
BS02 NAP C A6 A7 I14 N18 A19 M20 G43 R44 H45 T46 S63 S64 K76 I94 G96 G97 R98 V99 Q102 T123 A6 A7 I14 N18 A19 M20 G43 R44 H45 T46 S63 S64 K76 I94 G96 G97 R98 V99 Q102 T123
BS03 TOP C I5 A6 D27 F31 S49 I50 I94 I5 A6 D27 F31 S49 I50 I94
Gene Ontology
Molecular Function
GO:0004146 dihydrofolate reductase activity
GO:0005515 protein binding
GO:0005542 folic acid binding
GO:0016491 oxidoreductase activity
GO:0050661 NADP binding
GO:0051870 methotrexate binding
GO:0051871 dihydrofolic acid binding
GO:0070401 NADP+ binding
GO:0070402 NADPH binding
Biological Process
GO:0006730 one-carbon metabolic process
GO:0009257 10-formyltetrahydrofolate biosynthetic process
GO:0009410 response to xenobiotic stimulus
GO:0031427 response to methotrexate
GO:0046452 dihydrofolate metabolic process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046655 folic acid metabolic process
GO:0046656 folic acid biosynthetic process
GO:0046677 response to antibiotic
Cellular Component
GO:0005829 cytosol

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:7mym, PDBe:7mym, PDBj:7mym
PDBsum7mym
PubMed35562546
UniProtP0ABQ4|DYR_ECOLI Dihydrofolate reductase (Gene Name=folA)

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