Structure of PDB 4h96 Chain A

Receptor sequence

>4h96A (length=189) Species: 5476 (Candida albicans)

PNVAIIVAALKPALGIGYKGKMPWRLRKEIRYFKDVTTRTTKPNTRNAVI
MGRKTWESIPQKFRPLPDRLNIILSRSYENEIIDDNIIHASSIESSLNLV
SDVERVFIIGGAEIYNELINNSLVSHLLITEIEHPSPESIEMDTFLKFPL
ESWTKQPKSELQKFVGDTVLEDDIKEGDFTYNYTLWTRK

3D structure

• PDB: 4h96 Structural analysis of the active sites of dihydrofolate reductase from two species of Candida uncovers ligand-induced conformational changes shared among species.
• Chain: A
• Resolution: 2.6 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): M22 W24 E29 I30 F33 L66 V106 T130
• 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	A	V10 A11 I19 G23 K24 M25 R56 K57 T58 S78 R79 S94 I112 G114 A115 E116 I117	V7 A8 I16 G20 K21 M22 R53 K54 T55 S75 R76 S91 I109 G111 A112 E113 I114
BS02	14Q	A	I9 V10 E32 I33 F36 I62 I112	I6 V7 E29 I30 F33 I59 I109

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:4h96, PDBe:4h96, PDBj:4h96
• PDBsum: 4h96
• PubMed: 23375226
• UniProt: P22906|DYR_CANAX Dihydrofolate reductase (Gene Name=DFR1)