Structure of PDB 4h97 Chain B

Receptor sequence
>4h97B (length=190) Species: 5476 (Candida albicans) [Search protein sequence]
KPNVAIIVAALKPALGIGYKGKMPWRLRKEIRYFKDVTTRTTKPNTRNAV
IMGRKTWESIPQKFRPLPDRLNIILSRSYENEIIDDNIIHASSIESSLNL
VSDVERVFIIGGAEIYNELINNSLVSHLLITEIEHPSPESIEMDTFLKFP
LESWTKQPKSELQKFVGDTVLEDDIKEGDFTYNYTLWTRK
3D structure
PDB4h97 Structural analysis of the active sites of dihydrofolate reductase from two species of Candida uncovers ligand-induced conformational changes shared among species.
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 V10 A11 I19 G23 K24 M25 R56 K57 T58 L77 S78 R79 S94 I112 G114 A115 E116 I117 Y118 V8 A9 I17 G21 K22 M23 R54 K55 T56 L75 S76 R77 S92 I110 G112 A113 E114 I115 Y116
BS02 53S B I9 V10 E32 F36 F66 I112 I7 V8 E30 F34 F64 I110 MOAD: ic50=22nM
BindingDB: IC50=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

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Cellular Component
External links
PDB RCSB:4h97, PDBe:4h97, PDBj:4h97
PDBsum4h97
PubMed23375226
UniProtP22906|DYR_CANAX Dihydrofolate reductase (Gene Name=DFR1)

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