Structure of PDB 1s3y Chain A

Receptor sequence
>1s3yA (length=206) Species: 4754 (Pneumocystis carinii) [Search protein sequence]
MNQQKSLTLIVALTTSYGIGRSNSLPWKLKKEISYFKRVTSFVPTFDSFE
SMNVVLMGRKTWESIPLQFRPLKGRINVVITRNESLDLGNGIHSAKSLDH
ALELLYRTYGSESSVQINRIFVIGGAQLYKAAMDHPKLDRIMATIIYKDI
HCDVFFPLKFRDKEWSSVWKKEKHSDLESWVGTKVPHGKINEDGFDYEFE
MWTRDL
3D structure
PDB1s3y Structure determination of tetrahydroquinazoline antifolates in complex with human and Pneumocystis carinii dihydrofolate reductase: correlations between enzyme selectivity and stereochemistry.
ChainA
Resolution2.25 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) L25 E32
Catalytic site (residue number reindexed from 1) L25 E32
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 NAP A N23 G58 R59 K60 T61 T81 R82 K96 G125 A126 Q127 N23 G58 R59 K60 T61 T81 R82 K96 G125 A126 Q127
BS02 TQT A I10 V11 E32 I33 F36 P66 I123 I10 V11 E32 I33 F36 P66 I123 MOAD: ic50=210nM
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1s3y, PDBe:1s3y, PDBj:1s3y
PDBsum1s3y
PubMed15039552
UniProtP16184|DYR_PNECA Dihydrofolate reductase

[Back to BioLiP]