Structure of PDB 1vj3 Chain A

Receptor sequence

>1vj3A (length=205) Species: 4754 (Pneumocystis carinii)

NQQKSLTLIVALTTSYGIGRSNSLPWKLKKEISYFKRVTSFVPTFDSFES
MNVVLMGRKTWESIPLQFRPLKGRINVVITRNESLDLGNGIHSAKSLDHA
LELLYRTYGSESSVQINRIFVIGGAQLYKAAMDHPKLDRIMATIIYKDIH
CDVFFPLKFRDKEWSSVWKKEKHSDLESWVGTKVPHGKINEDGFDYEFEM
WTRDL

3D structure

• PDB: 1vj3 Structural studies on bioactive compounds. 30. Crystal structure and molecular modeling studies on the Pneumocystis carinii dihydrofolate reductase cofactor complex with TAB, a highly selective antifolate.
• Chain: A
• Resolution: 2.1 Å

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 G58 R59 K60 T61 I80 T81 R82 I123 G125 A126 Q127 L128 Y129	A11 I18 N22 S23 G57 R58 K59 T60 I79 T80 R81 I122 G124 A125 Q126 L127 Y128
BS02	TAB	A	I10 L25 E32 I33 F36 K37 P66 F69 L72	I9 L24 E31 I32 F35 K36 P65 F68 L71	MOAD: ic50=0.17uM BindingDB: IC50=170nM

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:1vj3, PDBe:1vj3, PDBj:1vj3
• PDBsum: 1vj3
• PubMed: 10736154
• UniProt: P16184|DYR_PNECA Dihydrofolate reductase