Structure of PDB 1cd2 Chain A

Receptor sequence
>1cd2A (length=206) Species: 4754 (Pneumocystis carinii) [Search protein sequence]
MNQQKSLTLIVALTTSYGIGRSNSLPWKLKKEISYFKRVTSFVPTFDSFE
SMNVVLMGRKTWESIPLQFRPLKGRINVVITRNESLDLGNGIHSAKSLDH
ALELLYRTYGSESSVQINRIFVIGGAQLYKAAMDHPKLDRIMATIIYKDI
HCDVFFPLKFRDKEWSSVWKKEKHSDLESWVGTKVPHGKINEDGFDYEFE
MWTRDL
3D structure
PDB1cd2 Ligand-induced conformational changes in the crystal structures of Pneumocystis carinii dihydrofolate reductase complexes with folate and NADP+.
ChainA
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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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 V11 A12 I19 N23 S24 G58 R59 K60 T61 I80 T81 R82 I123 G125 A126 Q127 L128 Y129 V11 A12 I19 N23 S24 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:1cd2, PDBe:1cd2, PDBj:1cd2
PDBsum1cd2
PubMed10194348
UniProtP16184|DYR_PNECA Dihydrofolate reductase

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