Structure of PDB 3h2o Chain A

Receptor sequence
>3h2oA (length=264) Species: 191218 (Bacillus anthracis str. A2012) [Search protein sequence]
KWDYDLRCGEYTLNLNEKTLIMGILNVTPDSFSDGGSYNEVDAAVRHAKE
MRDEGAHIIDIGKVSVEEEIKRVVPMIQAVSKEVKLPISIDTYKAEVAKQ
AIEAGAHIINDIWGAKAEPKIAEVAAHYDVPIILMHNRDNMNYRNLMADM
IADLYDSIKIAKDAGVRDENIILDPGIGFAKTPEQNLEAMRNLEQLNVLG
YPVLLGTSRKSFIGHVLDLPVEERLEGTGATVCLGIEKGCEFVRVHDVKE
MSRMAKMMDAMIGK
3D structure
PDB3h2o Structural studies of pterin-based inhibitors of dihydropteroate synthase.
ChainA
Resolution2.7 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 D53 K210 R244
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 B63 A N120 I122 M145 D184 G188 G216 K220 S221 R254 N110 I112 M135 D174 G178 G206 K210 S211 R244 PDBbind-CN: -logKd/Ki=4.59,IC50=25.9uM
BindingDB: IC50=25900nM
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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Cellular Component
External links
PDB RCSB:3h2o, PDBe:3h2o, PDBj:3h2o
PDBsum3h2o
PubMed19899766
UniProtQ81VW8

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