Structure of PDB 1tx2 Chain A Binding Site BS01

Receptor Information
>1tx2 Chain A (length=269) Species: 191218 (Bacillus anthracis str. A2012) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
KWDYDLRCGEYTLNLNEKTLIMGILNVTPDSFSDGGSYNEVDAAVRHAKE
MRDEGAHIIDIGGESFAKVSVEEEIKRVVPMIQAVSKEVKLPISIDTYKA
EVAKQAIEAGAHIINDIWGAKAEPKIAEVAAHYDVPIILMHNRDNMNYRN
LMADMIADLYDSIKIAKDAGVRDENIILDPGIGFAKTPEQNLEAMRNLEQ
LNVLGYPVLLGTSRKSFIGHVLDLPVEERLEGTGATVCLGIEKGCEFVRV
HDVKEMSRMAKMMDAMIGK
Ligand information
Ligand ID680
InChIInChI=1S/C5H7N5O3/c1-7-3-2(10(12)13)4(11)9-5(6)8-3/h1H3,(H4,6,7,8,9,11)
InChIKeyNMCMUSAXKISTKW-UHFFFAOYSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0CNC1=C(C(=O)NC(=N1)N)[N+](=O)[O-]
CACTVS 3.341CNC1=C(C(=O)NC(=N1)N)[N+]([O-])=O
ACDLabs 10.04O=C1C([N+]([O-])=O)=C(N=C(N)N1)NC
FormulaC5 H7 N5 O3
Name6-METHYLAMINO-5-NITROISOCYTOSINE
ChEMBLCHEMBL56190
DrugBankDB03705
ZINCZINC000018086542
PDB chain1tx2 Chain A Residue 502 [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]
PDB1tx2 Crystal Structure of 7,8-Dihydropteroate Synthase from Bacillus anthracis; Mechanism and Novel Inhibitor Design.
Resolution1.83 Å
Binding residue
(original residue number in PDB)		D101 N120 I122 M145 D184 F189 G216 K220 R254
Binding residue
(residue number reindexed from 1)		D96 N115 I117 M140 D179 F184 G211 K215 R249
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) V28 D54 K220 R254
Catalytic site (residue number reindexed from 1) V27 D53 K215 R249
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:1tx2, PDBe:1tx2, PDBj:1tx2
PDBsum1tx2
PubMed15341734
UniProtQ81VW8

[Back to BioLiP]