Structure of PDB 3h21 Chain B Binding Site BS01

Receptor Information
>3h21 Chain B (length=256) Species: 191218 (Bacillus anthracis str. A2012) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KWDYDLRCGEYTLNLNEKTLIMGILNDGGSYNEVDAAVRHAKEMRDEGAH
IIDIGGSVEEEIKRVVPMIQAVSKEVKLPISIDTYKAEVAKQAIEAGAHI
INDIWGAKAEPKIAEVAAHYDVPIILMHNRDNMNYRNLMADMIADLYDSI
KIAKDAGVRDENIILDPGIGFAKTPEQNLEAMRNLEQLNVLGYPVLLGTS
RKSFIGHVLDLPVEERLEGTGATVCLGIEKGCEFVRVHDVKEMSRMAKMM
DAMIGK
Ligand information
Ligand IDB52
InChIInChI=1S/C10H11N5O4/c1-3(9(18)19)5-6(16)4-7(15(2)14-5)12-10(11)13-8(4)17/h3H,1-2H3,(H,18,19)(H3,11,12,13,17)/t3-/m1/s1
InChIKeyXUKTUWRGSZSUGO-GSVOUGTGSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=C(O)C(C1=NN(C=2N=C(NC(=O)C=2C1=O)N)C)C
CACTVS 3.341C[CH](C(O)=O)C1=NN(C)C2=C(C(=O)NC(=N2)N)C1=O
CACTVS 3.341C[C@@H](C(O)=O)C1=NN(C)C2=C(C(=O)NC(=N2)N)C1=O
OpenEye OEToolkits 1.5.0C[C@H](C1=NN(C2=C(C1=O)C(=O)NC(=N2)N)C)C(=O)O
OpenEye OEToolkits 1.5.0CC(C1=NN(C2=C(C1=O)C(=O)NC(=N2)N)C)C(=O)O
FormulaC10 H11 N5 O4
Name(2R)-2-(7-amino-1-methyl-4,5-dioxo-1,4,5,6-tetrahydropyrimido[4,5-c]pyridazin-3-yl)propanoic acid
ChEMBL
DrugBank
ZINCZINC000039233407
PDB chain3h21 Chain B Residue 278 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB3h21 Structural studies of pterin-based inhibitors of dihydropteroate synthase.
Resolution2.32 Å
Binding residue
(original residue number in PDB)		D101 N120 I122 M145 D184 F189 G216 K220 R254
Binding residue
(residue number reindexed from 1)		D83 N102 I104 M127 D166 F171 G198 K202 R236
Annotation score1
Binding affinityMOAD: ic50=19.8uM
BindingDB: IC50=19800nM
Enzymatic activity
Catalytic site (original residue number in PDB) D54 K220 R254
Catalytic site (residue number reindexed from 1) D46 K202 R236
Enzyme Commision number 2.5.1.15: dihydropteroate synthase.
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3h21, PDBe:3h21, PDBj:3h21
PDBsum3h21
PubMed19899766
UniProtQ81VW8

[Back to BioLiP]