Structure of PDB 4daf Chain B

Receptor sequence
>4dafB (length=252) Species: 191218 (Bacillus anthracis str. A2012) [Search protein sequence]
KWDYDLRCGEYTLNLNEKTLIMGILNSYNEVDAAVRHAKEMRDEGAHIID
IGSVEEEIKRVVPMIQAVSKEVKLPISIDTYKAEVAKQAIEAGAHIINDI
WGAKAEPKIAEVAAHYDVPIILMHNRDNMNYRNLMADMIADLYDSIKIAK
DAGVRDENIILDPGIGFAKTPEQNLEAMRNLEQLNVLGYPVLLGTSRKSF
IGHVLDLPVEERLEGTGATVCLGIEKGCEFVRVHDVKEMSRMAKMMDAMI
GK
3D structure
PDB4daf Structure-Based Design of Novel Pyrimido[4,5-c]pyridazine Derivatives as Dihydropteroate Synthase Inhibitors with Increased Affinity.
ChainB
Resolution2.501 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D54 K220 R254
Catalytic site (residue number reindexed from 1) D43 K198 R232
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 0J4 B D101 N120 I122 M145 D184 F189 G216 K220 R254 D79 N98 I100 M123 D162 F167 G194 K198 R232 MOAD: Kd=0.076uM
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:4daf, PDBe:4daf, PDBj:4daf
PDBsum4daf
PubMed22416048
UniProtQ81VW8

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