Structure of PDB 4gh8 Chain B

Receptor sequence
>4gh8B (length=162) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MISLIAALAVDRVIGMENAMPWPPLPADLAWFKRNTLNKPVIMGRHTWES
IPEKNRPLPGRKNIILSSQPGTDDRVTWVKSVDEAIAACGDVPEIMVIGG
GRVYEQFLPKAQKLYLTHIDAEVEGDTHFPDYEPDDWESVFSEFHDADAQ
NSHSYCFEILER
3D structure
PDB4gh8 Functional significance of evolving protein sequence in dihydrofolate reductase from bacteria to humans.
ChainB
Resolution1.85 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) I5 M20 W22 D28 L29 F32 L58 I95 T117
Catalytic site (residue number reindexed from 1) I5 M20 W22 D28 L29 F32 L58 I95 T117
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 MTX B I5 A6 A7 M20 D28 L29 F32 K33 P52 N55 R61 I5 A6 A7 M20 D28 L29 F32 K33 P52 N55 R61 BindingDB: IC50=8.8nM,EC50=1nM
BS02 NDP B A6 A7 I14 N18 A19 G44 R45 H46 T47 L66 S67 S68 K80 I98 G100 G101 R102 V103 Q106 A6 A7 I14 N18 A19 G44 R45 H46 T47 L66 S67 S68 K80 I98 G100 G101 R102 V103 Q106 MOAD: Kd=2.6uM
BS03 CA B E53 R56 E53 R56
Gene Ontology
Molecular Function
GO:0004146 dihydrofolate reductase activity
GO:0050661 NADP binding
Biological Process
GO:0046654 tetrahydrofolate biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4gh8, PDBe:4gh8, PDBj:4gh8
PDBsum4gh8
PubMed23733948
UniProtP0ABQ4|DYR_ECOLI Dihydrofolate reductase (Gene Name=folA)

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