Structure of PDB 1dyj Chain B

Receptor sequence

>1dyjB (length=159) Species: 562 (Escherichia coli)

MISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLDKPVIMGRHTWESI
GRPLPGRKNIILSSQPGTDDRVTWVKSVDEAIAACGDVPEIMVIGGGRVY
EQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSHS
YCFEILERR

3D structure

• PDB: 1dyj Isomorphous crystal structures of Escherichia coli dihydrofolate reductase complexed with folate, 5-deazafolate, and 5,10-dideazatetrahydrofolate: mechanistic implications.
• Chain: B
• Resolution: 1.85 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): I5 M20 W22 D27 L28 F31 L54 I91 T113
• Catalytic site (residue number reindexed from 1): I5 M20 W22 D27 L28 F31 L54 I91 T113
• 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	DDF	B	A6 A7 D27 F31 K32 R57 Y100	A6 A7 D27 F31 K32 R57 Y100

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

External links

• PDB: RCSB:1dyj, PDBe:1dyj, PDBj:1dyj
• PDBsum: 1dyj
• PubMed: 7873554
• UniProt: P0ABQ4|DYR_ECOLI Dihydrofolate reductase (Gene Name=folA)