Structure of PDB 1dyr Chain A

Receptor sequence
>1dyrA (length=205) Species: 4754 (Pneumocystis carinii) [Search protein sequence]
NQQKSLTLIVALTTSYGIGRSNSLPWKLKKEISYFKRVTSFVPTFDSFES
MNVVLMGRKTWESIPLQFRPLKGRINVVITRNESLDLGNGIHSAKSLDHA
LELLYRTYGSESSVQINRIFVIGGAQLYKAAMDHPKLDRIMATIIYKDIH
CDVFFPLKFRDKEWSSVWKKEKHSDLESWVGTKVPHGKINEDGFDYEFEM
WTRDL
3D structure
PDB1dyr The structure of Pneumocystis carinii dihydrofolate reductase to 1.9 A resolution.
ChainA
Resolution1.86 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) L25 E32
Catalytic site (residue number reindexed from 1) L24 E31
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 A12 I19 N23 S24 L25 G58 R59 K60 T61 I80 T81 R82 N83 I123 G125 A126 Q127 L128 A11 I18 N22 S23 L24 G57 R58 K59 T60 I79 T80 R81 N82 I122 G124 A125 Q126 L127
BS02 TOP A I10 L25 E32 F36 I123 I9 L24 E31 F35 I122 MOAD: ic50=20uM
BindingDB: IC50=12000nM,Ki=280000nM
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:1dyr, PDBe:1dyr, PDBj:1dyr
PDBsum1dyr
PubMed7866743
UniProtP16184|DYR_PNECA Dihydrofolate reductase

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