Structure of PDB 3h2m Chain A

Receptor sequence
>3h2mA (length=270) Species: 191218 (Bacillus anthracis str. A2012) [Search protein sequence]
MKWDYDLRCGEYTLNLNEKTLIMGILNVTPDSFSDGGSYNEVDAAVRHAK
EMRDEGAHIIDIGGESFAKVSVEEEIKRVVPMIQAVSKEVKLPISIDTYK
AEVAKQAIEAGAHIINDIWGAKAEPKIAEVAAHYDVPIILMHNRDNMNYR
NLMADMIADLYDSIKIAKDAGVRDENIILDPGIGFAKTPEQNLEAMRNLE
QLNVLGYPVLLGTSRKSFIGHVLDLPVEERLEGTGATVCLGIEKGCEFVR
VHDVKEMSRMAKMMDAMIGK
3D structure
PDB3h2m Structural studies of pterin-based inhibitors of dihydropteroate synthase.
ChainA
Resolution2.31 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) V28 D54 K216 R250
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 B61 A D101 N120 I122 M145 D184 F189 G216 K220 R254 D97 N116 I118 M141 D180 F185 G212 K216 R250 MOAD: ic50=215uM
PDBbind-CN: -logKd/Ki=3.67,IC50=215uM
BindingDB: IC50=215000nM
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:3h2m, PDBe:3h2m, PDBj:3h2m
PDBsum3h2m
PubMed19899766
UniProtQ81VW8

[Back to BioLiP]