Structure of PDB 4klx Chain B

Receptor sequence
>4klxB (length=160) Species: 1773 (Mycobacterium tuberculosis) [Search protein sequence]
HMVGLIWAQATSGVIGRGGDIPWRLPEDQAHFREITMGHTIVMGRRTWDS
LPAKVRPLPGRRNVVLSRQADFMASGAEVVGSLEEALTSPETWVIGGGQV
YALALPYATRCEVTEVDIGLPREAGDALAPVLDETWRGETGEWRFSRSGL
RYRLYSYHRS
3D structure
PDB4klx Mycobacterium tuberculosis Dihydrofolate Reductase Reveals Two Conformational States and a Possible Low Affinity Mechanism to Antifolate Drugs.
ChainB
Resolution1.23 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 I20 W22 D27 Q28 F31 L57 T91 T113
Catalytic site (residue number reindexed from 1) I6 I21 W23 D28 Q29 F32 L58 T92 T114
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 ATR B G43 R44 R45 T46 L65 S66 R67 G80 G96 G97 Q98 V99 G44 R45 R46 T47 L66 S67 R68 G81 G97 G98 Q99 V100
Gene Ontology
Molecular Function
GO:0004146 dihydrofolate reductase activity
GO:0016491 oxidoreductase activity
GO:0050661 NADP binding
GO:0070401 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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Cellular Component
External links
PDB RCSB:4klx, PDBe:4klx, PDBj:4klx
PDBsum4klx
PubMed24210757
UniProtP9WNX1|DYR_MYCTU Dihydrofolate reductase (Gene Name=folA)

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