Structure of PDB 2w3w Chain A

Receptor sequence
>2w3wA (length=164) Species: 1764 (Mycobacterium avium) [Search protein sequence]
RAEVGLVWAQSTSGVIGRGGDIPWSVPEDLTRFKEVTMGHTVIMGRRTWE
SLPAKVRPLPGRRNVVVSRRPDFVAEGARVAGSLEAALAYAGSDPAPWVI
GGAQIYLLALPHATRCEVTEIEIDLRRDDDDALAPALDDSWVGETGEWLA
SRSGLRYRFHSYRR
3D structure
PDB2w3w Structural Basis for Selective Inhibition of Mycobacterium Avium Dihydrofolate Reductase by a Lipophilic Antifolate
ChainA
Resolution1.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) V9 I24 W26 D31 L32 F35 L61 P99 T121
Catalytic site (residue number reindexed from 1) V7 I22 W24 D29 L30 F33 L59 P97 T119
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 VG9 A V9 W10 A11 I24 D31 L32 F35 L61 I102 R166 V7 W8 A9 I22 D29 L30 F33 L59 I100 R164
BS02 NDP A W10 A11 I18 G22 D23 I24 G47 R48 R49 T50 V69 S70 R71 R72 I102 G104 A105 Q106 I107 L110 W8 A9 I16 G20 D21 I22 G45 R46 R47 T48 V67 S68 R69 R70 I100 G102 A103 Q104 I105 L108
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
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:0005829 cytosol

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External links
PDB RCSB:2w3w, PDBe:2w3w, PDBj:2w3w
PDBsum2w3w
PubMed
UniProtO30463

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