Structure of PDB 1ly3 Chain A

Receptor sequence

>1ly3A (length=206) Species: 4754 (Pneumocystis carinii)

MNQQKSLTLIVALTTSYGIGRSNSLPWKLKKEISYFKRVTSFVPTFDSFE
SMNVVLMGRKTWESIPLQFRPLKGRINVVITRNESLDLGNGIHSAKSLDH
ALELLYRTYGSESSVQINRIFVIGGAQLYKAAMDHPKLDRIMATIIYKDI
HCDVFFPLKFRDKEWSSVWKKEKHSDLESWVGTKVPHGKINEDGFDYEFE
MWTRDL

3D structure

• PDB: 1ly3 Analysis of quinazoline and pyrido[2,3-d]pyrimidine N9-C10 reversed-bridge antifolates in complex with NADP+ and Pneumocystis carinii dihydrofolate reductase.
• Chain: A
• Resolution: 1.9 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	NAP	A	A12 I19 N23 S24 L25 G58 R59 K60 T61 I80 T81 R82 I123 G125 A126 Q127 L128	A12 I19 N23 S24 L25 G58 R59 K60 T61 I80 T81 R82 I123 G125 A126 Q127 L128
BS02	COG	A	I10 V11 L25 E32 I33 F36 P66 F69 I123	I10 V11 L25 E32 I33 F36 P66 F69 I123	MOAD: ic50=87nM BindingDB: IC50=87nM

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:1ly3, PDBe:1ly3, PDBj:1ly3
• PDBsum: 1ly3
• PubMed: 12198294
• UniProt: P16184|DYR_PNECA Dihydrofolate reductase