Structure of PDB 3qfx Chain B

Receptor sequence
>3qfxB (length=218) Species: 31286 (Trypanosoma brucei rhodesiense) [Search protein sequence]
PPLRPFSVVVASDEKGGIGDGGTIPWEIPEDMQYFRRVTTNLRGKNVKPS
PSKRNAVVMGRKTWDSLPPKFRPLSNRLNVVLSRSATKEQLLAGIPDPIK
RAEAANDVVAVNGGLEDALRMLVSKEHTSSIETVFCIGGGTIYKQALCAP
CVNVLQAIHRTVVRPASNSCSVFFDIPAAGTKTPEGLELVRESITDERVS
TGAGGKKYQFEKLVPRNS
3D structure
PDB3qfx Trypanosomal dihydrofolate reductase reveals natural antifolate resistance
ChainB
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) I47 D54
Catalytic site (residue number reindexed from 1) I24 D31
Enzyme Commision number 1.5.1.3: dihydrofolate reductase.
2.1.1.45: thymidylate synthase.
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 B V33 A34 I41 G44 G45 T46 G83 R84 K85 T86 L105 S106 R107 G136 G137 I160 G162 G163 T164 I165 Y166 V10 A11 I18 G21 G22 T23 G60 R61 K62 T63 L82 S83 R84 G113 G114 I137 G139 G140 T141 I142 Y143
BS02 CP6 B V32 V33 A34 D54 F58 T86 L90 V9 V10 A11 D31 F35 T63 L67 MOAD: Ki=24.2nM
Gene Ontology
Molecular Function
GO:0004146 dihydrofolate reductase activity
GO:0050661 NADP binding
Biological Process
GO:0046654 tetrahydrofolate biosynthetic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3qfx, PDBe:3qfx, PDBj:3qfx
PDBsum3qfx
PubMed21650210
UniProtQ27783|DRTS_TRYBB Bifunctional dihydrofolate reductase-thymidylate synthase

[Back to BioLiP]