Structure of PDB 5uio Chain B

Receptor sequence

>5uioB (length=160) Species: 562 (Escherichia coli)

MMISLIAALAVDRVIGMENAMPWNLPADLAWFKRNTLNKPVIMGRHTWES
IGRPLPGRKNIILSSQPGTDDRVTWVKSVDEAIAACGDVPEIMVIGGGRV
YEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQNSH
SYCFEILERR

3D structure

• PDB: 5uio A Structural Basis for Biguanide Activity.
• Chain: B
• Resolution: 1.929 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): I6 M21 W23 D28 L29 F32 L55 I92 T114
• 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	LG3	B	A6 D27 F31	A7 D28 F32

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:5uio, PDBe:5uio, PDBj:5uio
• PDBsum: 5uio
• PubMed: 28766937
• UniProt: P0ABQ4|DYR_ECOLI Dihydrofolate reductase (Gene Name=folA)