Structure of PDB 7nae Chain A

Receptor sequence
>7naeA (length=159) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWESI
GRPLPGRKNIILSSQPGTDDRVTWVKSVDEAIAACGDVPEIMVIGGGRVY
EQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHS
YCFEILERR
3D structure
PDB7nae Structure-guided functional studies of plasmid-encoded dihydrofolate reductases reveal a common mechanism of trimethoprim resistance in Gram-negative pathogens.
ChainA
Resolution2.35 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 A I5 A6 W22 D27 F31 I94 I5 A6 W22 D27 F31 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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Cellular Component
External links
PDB RCSB:7nae, PDBe:7nae, PDBj:7nae
PDBsum7nae
PubMed35562546
UniProtP0ABQ4|DYR_ECOLI Dihydrofolate reductase (Gene Name=folA)

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