Structure of PDB 2fzh Chain A

Receptor sequence

>2fzhA (length=206) Species: 4754 (Pneumocystis carinii)

MNQQKSLTLIVALTTSYGIGRSNSLPWKLKKEISYFKRVTSFVPTFDSFE
SMNVVLMGRKTWESIPLQFRPLKGRINVVITRNESLDLGNGIHSAKSLDH
ALELLYRTYGSESSVQINRIFVIGGAQLYKAAMDHPKLDRIMATIIYKDI
HCDVFFPLKFRDKEWSSVWKKEKHSDLESWVGTKVPHGKINEDGFDYEFE
MWTRDL

3D structure

• PDB: 2fzh New insights into DHFR interactions: analysis of Pneumocystis carinii and mouse DHFR complexes with NADPH and two highly potent 5-(omega-carboxy(alkyloxy) trimethoprim derivatives reveals conformational correlations with activity and novel parallel ring stacking interactions.
• Chain: A
• Resolution: 2.1 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	V11 A12 I19 G20 S24 L25 G58 R59 K60 T61 I80 T81 R82 K96 I123 G125 A126 Q127 L128	V11 A12 I19 G20 S24 L25 G58 R59 K60 T61 I80 T81 R82 K96 I123 G125 A126 Q127 L128
BS02	DH1	A	I10 V11 A12 E32 I33 F36 K37 F69 L72 R75 I123	I10 V11 A12 E32 I33 F36 K37 F69 L72 R75 I123	MOAD: ic50=0.049nM

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:2fzh, PDBe:2fzh, PDBj:2fzh
• PDBsum: 2fzh
• PubMed: 17019704
• UniProt: P16184|DYR_PNECA Dihydrofolate reductase