Structure of PDB 1daj Chain A

Receptor sequence

>1dajA (length=206) Species: 4754 (Pneumocystis carinii)

MNQQKSLTLIVALTTSYGIGRSNSLPWKLKKEISYFKRVTSFVPTFDSFE
SMNVVLMGRKTWESIPLQFRPLKGRINVVITRNESLDLGNGIHSAKSLDH
ALELLYRTYGSESSVQINRIFVIGGAQLYKAAMDHPKLDRIMATIIYKDI
HCDVFFPLKFRDKEWSSVWKKEKHSDLESWVGTKVPHGKINEDGFDYEFE
MWTRDL

3D structure

• PDB: 1daj Comparison of ternary complexes of Pneumocystis carinii and wild-type human dihydrofolate reductase with coenzyme NADPH and a novel classical antitumor furo[2,3-d]pyrimidine antifolate.
• Chain: A
• Resolution: 2.3 Å

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	NDP	A	A12 I19 N23 S24 G58 R59 K60 T61 R82 N83 I123 G125 A126 Q127 L128 Y129 V154	A12 I19 N23 S24 G58 R59 K60 T61 R82 N83 I123 G125 A126 Q127 L128 Y129 V154
BS02	MOT	A	I10 V11 E32 I33 F36 I65 F69 L72 R75 I123	I10 V11 E32 I33 F36 I65 F69 L72 R75 I123	MOAD: Ki=6.5nM

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:1daj, PDBe:1daj, PDBj:1daj
• PDBsum: 1daj
• PubMed: 15299851
• UniProt: P16184|DYR_PNECA Dihydrofolate reductase