Structure of PDB 3h22 Chain A

Receptor sequence
>3h22A (length=261) Species: 191218 (Bacillus anthracis str. A2012) [Search protein sequence]
KWDYDLRCGEYTLNLNEKTLIMGILNVTPDSFGGSYNEVDAAVRHAKEMR
DEGAHIIDIGGSVEEEIKRVVPMIQAVSKEVKLPISIDTYKAEVAKQAIE
AGAHIINDIWGAKAEPKIAEVAAHYDVPIILMHNRDNMNYRNLMADMIAD
LYDSIKIAKDAGVRDENIILDPGIGFAKTPEQNLEAMRNLEQLNVLGYPV
LLGTSRKSFIGHVLDLPVEERLEGTGATVCLGIEKGCEFVRVHDVKEMSR
MAKMMDAMIGK
3D structure
PDB3h22 Structural studies of pterin-based inhibitors of dihydropteroate synthase.
ChainA
Resolution2.4 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) V27 D51 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 B53 A D101 N120 I122 M145 D184 F189 G216 K220 R254 D88 N107 I109 M132 D171 F176 G203 K207 R241 MOAD: ic50=8uM
PDBbind-CN: -logKd/Ki=5.10,IC50=8uM
BindingDB: IC50=8000nM
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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External links
PDB RCSB:3h22, PDBe:3h22, PDBj:3h22
PDBsum3h22
PubMed19899766
UniProtQ81VW8

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