Structure of PDB 3h23 Chain A

Receptor sequence

>3h23A (length=274) Species: 191218 (Bacillus anthracis str. A2012)

KWDYDLRCGEYTLNLNEKTLIMGILNVTPDSFSDGGSYNEVDAAVRHAKE
MRDEGAHIIDIGGESTRPGFAKVSVEEEIKRVVPMIQAVSKEVKLPISID
TYKAEVAKQAIEAGAHIINDIWGAKAEPKIAEVAAHYDVPIILMHNRDNM
NYRNLMADMIADLYDSIKIAKDAGVRDENIILDPGIGFAKTPEQNLEAMR
NLEQLNVLGYPVLLGTSRKSFIGHVLDLPVEERLEGTGATVCLGIEKGCE
FVRVHDVKEMSRMAKMMDAMIGKG

3D structure

• PDB: 3h23 Structural studies of pterin-based inhibitors of dihydropteroate synthase.
• Chain: A
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): V28 D54 K220 R254
• Catalytic site (residue number reindexed from 1): V27 D53 K219 R253
• 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	B54	A	T67 P69 D101 N120 I122 M145 D184 G216 K220 R254 H256	T66 P68 D100 N119 I121 M144 D183 G215 K219 R253 H255	MOAD: ic50=19.3uM PDBbind-CN: -logKd/Ki=4.71,IC50=19.3uM BindingDB: IC50=19300nM

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

External links

• PDB: RCSB:3h23, PDBe:3h23, PDBj:3h23
• PDBsum: 3h23
• PubMed: 19899766
• UniProt: Q81VW8