Structure of PDB 4d8z Chain B Binding Site BS01

Receptor Information
>4d8z Chain B (length=258) Species: 191218 (Bacillus anthracis str. A2012) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KWDYDLRCGEYTLNLNEKTLIMGILNSDGGSYNEVDAAVRHAKEMRDEGA
HIIDIGGESVEEEIKRVVPMIQAVSKEVKLPISIDTYKAEVAKQAIEAGA
HIINDIWGAKAEPKIAEVAAHYDVPIILMHNRDNMNYRNLMADMIADLYD
SIKIAKDAGVRDENIILDPGIGFAKTPEQNLEAMRNLEQLNVLGYPVLLG
TSRKSFIGHVLDLPVEERLEGTGATVCLGIEKGCEFVRVHDVKEMSRMAK
MMDAMIGK
Ligand information
Ligand ID0J2
InChIInChI=1S/C10H11N5O4/c1-3(2-4(16)17)6-7(18)5-8(15-14-6)12-10(11)13-9(5)19/h3H,2H2,1H3,(H,16,17)(H4,11,12,13,15,18,19)/t3-/m1/s1
InChIKeyKXEAQLNQKVKEGT-GSVOUGTGSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6C[C@H](CC(=O)O)C1=NNC2=C(C1=O)C(=O)NC(=N2)N
CACTVS 3.370C[C@H](CC(O)=O)C1=NNC2=C(C(=O)NC(=N2)N)C1=O
ACDLabs 12.01O=C(O)CC(C1=NNC=2N=C(NC(=O)C=2C1=O)N)C
OpenEye OEToolkits 1.7.6CC(CC(=O)O)C1=NNC2=C(C1=O)C(=O)NC(=N2)N
CACTVS 3.370C[CH](CC(O)=O)C1=NNC2=C(C(=O)NC(=N2)N)C1=O
FormulaC10 H11 N5 O4
Name(3R)-3-(7-amino-4,5-dioxo-1,4,5,6-tetrahydropyrimido[4,5-c]pyridazin-3-yl)butanoic acid
ChEMBL
DrugBank
ZINCZINC000095920571
PDB chain4d8z Chain B Residue 306 [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]
PDB4d8z Structure-Based Design of Novel Pyrimido[4,5-c]pyridazine Derivatives as Dihydropteroate Synthase Inhibitors with Increased Affinity.
Resolution2.198 Å
Binding residue
(original residue number in PDB)		D101 N120 I122 M145 D184 F189 G216 K220 R254
Binding residue
(residue number reindexed from 1)		D85 N104 I106 M129 D168 F173 G200 K204 R238
Annotation score1
Binding affinityMOAD: Kd=0.51uM
Enzymatic activity
Catalytic site (original residue number in PDB) D54 K220 R254
Catalytic site (residue number reindexed from 1) D47 K204 R238
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:4d8z, PDBe:4d8z, PDBj:4d8z
PDBsum4d8z
PubMed22416048
UniProtQ81VW8

[Back to BioLiP]