Structure of PDB 3h26 Chain B

Receptor sequence
>3h26B (length=270) Species: 191218 (Bacillus anthracis str. A2012) [Search protein sequence]
HHSSGLVPMKWDYDLRCGEYTLNLNEKTLIMGILNVTPDGGSYNEVDAAV
RHAKEMRDEGAHIIDIGGEVSVEEEIKRVVPMIQAVSKEVKLPISIDTYK
AEVAKQAIEAGAHIINDIWGAKAEPKIAEVAAHYDVPIILMHNRDNMNYR
NLMADMIADLYDSIKIAKDAGVRDENIILDPGIGFAKTPEQNLEAMRNLE
QLNVLGYPVLLGTSRKSFIGHVLDLPVEERLEGTGATVCLGIEKGCEFVR
VHDVKEMSRMAKMMDAMIGK
3D structure
PDB3h26 Structural studies of pterin-based inhibitors of dihydropteroate synthase.
ChainB
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) V28 D54 K220 R254
Catalytic site (residue number reindexed from 1) V36 D58 K216 R250
Enzyme Commision number 2.5.1.15: dihydropteroate 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 B56 B D101 N120 I122 M145 D184 F189 G216 K220 R254 D97 N116 I118 M141 D180 F185 G212 K216 R250 MOAD: ic50=32.4uM
BindingDB: Kd=5260nM,IC50=32400nM
Gene Ontology
Molecular Function
GO:0004156 dihydropteroate synthase activity
GO:0016740 transferase activity
GO:0046872 metal ion binding
Biological Process
GO:0009396 folic acid-containing compound biosynthetic process
GO:0042558 pteridine-containing compound metabolic process
GO:0044237 cellular metabolic process
GO:0046654 tetrahydrofolate biosynthetic process
GO:0046656 folic acid biosynthetic process
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:3h26, PDBe:3h26, PDBj:3h26
PDBsum3h26
PubMed19899766
UniProtQ81VW8

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