Structure of PDB 1aoe Chain B

Receptor sequence

>1aoeB (length=192) Species: 5476 (Candida albicans)

MLKPNVAIIVAALKPALGIGYKGKMPWRLRKEIRYFKDVTTRTTKPNTRN
AVIMGRKTWESIPQKFRPLPDRLNIILSRSYENEIIDDNIIHASSIESSL
NLVSDVERVFIIGGAEIYNELINNSLVSHLLITEIEHPSPESIEMDTFLK
FPLESWTKQPKSELQKFVGDTVLEDDIKEGDFTYNYTLWTRK

3D structure

• PDB: 1aoe X-ray crystallographic studies of Candida albicans dihydrofolate reductase. High resolution structures of the holoenzyme and an inhibited ternary complex.
• Chain: B
• Resolution: 1.6 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): M25 W27 E32 I33 F36 L69 V109 T133
• 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	V10 A11 I19 G23 K24 M25 G55 R56 K57 T58 L77 S78 R79 I96 I112 G114 A115 E116 I117 E120	V10 A11 I19 G23 K24 M25 G55 R56 K57 T58 L77 S78 R79 I96 I112 G114 A115 E116 I117 E120
BS02	GW3	B	I9 V10 E32 F36 I112	I9 V10 E32 F36 I112	MOAD: Ki=0.22nM BindingDB: IC50=4nM,Ki=0.22nM

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:1aoe, PDBe:1aoe, PDBj:1aoe
• PDBsum: 1aoe
• PubMed: 9374515
• UniProt: P22906|DYR_CANAX Dihydrofolate reductase (Gene Name=DFR1)