Structure of PDB 3qlw Chain B

Receptor sequence

>3qlwB (length=190) Species: 5476 (Candida albicans)

KPNVAIIVAALKPALGIGYKGKMPWRLRKEIRYFKDVTTRTTKPNTRNAV
IMGRKTWESIPQKFRPLPDRLNIILSRSYENEIIDDNIIHASSIESSLNL
VSDVERVFIIGGAEIYNELINNSLVSHLLITEIEHPSPESIEMDTFLKFP
LESWTKQPKSELQKFVGDTVLEDDIKEGDFTYNYTLWTRK

3D structure

• PDB: 3qlw Crystal Structures of Candida albicans Dihydrofolate Reductase Bound to Propargyl-Linked Antifolates Reveal the Flexibility of Active Site Loop Residues Critical for Ligand Potency and Selectivity.
• Chain: B
• Resolution: 2.504 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): M25 W27 E32 I33 F36 L69 V109 T133
• Catalytic site (residue number reindexed from 1): M23 W25 E30 I31 F34 L67 V107 T131
• 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	NDP	B	A11 I19 G23 M25 G55 R56 K57 T58 L77 S78 R79 S94 I112 G114 A115 E116 I117 Y118	A9 I17 G21 M23 G53 R54 K55 T56 L75 S76 R77 S92 I110 G112 A113 E114 I115 Y116
BS02	N22	B	I9 V10 M25 E32 F36 I112	I7 V8 M23 E30 F34 I110	MOAD: ic50=100nM BindingDB: IC50=100nM

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:0046452 dihydrofolate metabolic process
• GO:0046654 tetrahydrofolate biosynthetic process
• GO:0046655 folic acid metabolic process

Cellular Component

• GO:0005739 mitochondrion

External links

• PDB: RCSB:3qlw, PDBe:3qlw, PDBj:3qlw
• PDBsum: 3qlw
• PubMed: 21726415
• UniProt: P22906|DYR_CANAX Dihydrofolate reductase (Gene Name=DFR1)