Structure of PDB 1tx0 Chain B

Receptor sequence
>1tx0B (length=261) Species: 191218 (Bacillus anthracis str. A2012) [Search protein sequence]
KWDYDLRCGEYTLNLNEKTLIMGILNVTPSDGGSYNEVDAAVRHAKEMRD
EGAHIIDIGGVSVEEEIKRVVPMIQAVSKEVKLPISIDTYKAEVAKQAIE
AGAHIINDIWGAKAEPKIAEVAAHYDVPIILMHNRDNMNYRNLMADMIAD
LYDSIKIAKDAGVRDENIILDPGIGFAKTPEQNLEAMRNLEQLNVLGYPV
LLGTSRKSFIGHVLDLPVEERLEGTGATVCLGIEKGCEFVRVHDVKEMSR
MAKMMDAMIGK
3D structure
PDB1tx0 Crystal Structure of 7,8-Dihydropteroate Synthase from Bacillus anthracis; Mechanism and Novel Inhibitor Design.
ChainB
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) V28 D54 K220 R254
Catalytic site (residue number reindexed from 1) V27 D50 K207 R241
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 PT1 B N120 M145 D184 F189 G216 K220 S221 R254 N107 M132 D171 F176 G203 K207 S208 R241
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:1tx0, PDBe:1tx0, PDBj:1tx0
PDBsum1tx0
PubMed15341734
UniProtQ81VW8

[Back to BioLiP]