Structure of PDB 4qjz Chain D

Receptor sequence
>4qjzD (length=206) Species: 4754 (Pneumocystis carinii) [Search protein sequence]
MNQQKSLTLIVALTTSYGIGRSNSLPWKLKKEISYFKRVTSFVPTFDSFE
SMNVVLMGRKTWESIPLQFRPLKGRINVVITRNESLDLGNGIHSAKSLDH
ALELLYRTYGSESSVQINRIFVIGGAQLYKAAMDHPKLDRIMATIIYKDI
HCDVFFPLKFRDKEWSSVWKKEKHSDLESWVGTKVPHGKINEDGFDYEFE
MWTRDL
3D structure
PDB4qjz Structure-activity correlations for three pyrido[2,3-d]pyrimidine antifolates binding to human and Pneumocystis carinii dihydrofolate reductase.
ChainD
Resolution1.61 Å
3D
structure
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Enzymatic activity
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 33M D I10 V11 A12 L25 E32 I33 F36 I123 I10 V11 A12 L25 E32 I33 F36 I123
BS02 NDP D V11 A12 I19 S24 L25 G58 R59 K60 T61 I80 T81 R82 I123 G125 A126 Q127 L128 Y129 V11 A12 I19 S24 L25 G58 R59 K60 T61 I80 T81 R82 I123 G125 A126 Q127 L128 Y129
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

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Cellular Component
External links
PDB RCSB:4qjz, PDBe:4qjz, PDBj:4qjz
PDBsum4qjz
PubMed26057816
UniProtP16184|DYR_PNECA Dihydrofolate reductase

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