Structure of PDB 1ad4 Chain A

Receptor sequence
>1ad4A (length=251) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
TKTKIMGILNVNVESAVTRVKAMMDEGADIIDVGGVSTRPGHEMITVEEE
LNRVLPVVEAIVGFDVKISVDTFRSEVAEACLKLGVDIINDQWAGLYDHR
MFQVVAKYDAEIVLMHNGNGNRDEPVVEEMLTSLLAQAHQAKIAGIPSNK
IWLDPGIGFAKTRNEEAEVMARLDELVATEYPVLLATSRKRFTKEMMGYD
TTPVERDEVTAATTAYGIMKGVRAVRVHNVELNAKLAKGIDFLKENENAR
H
3D structure
PDB1ad4 Structure and function of the dihydropteroate synthase from Staphylococcus aureus.
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) K203 R239
Catalytic site (residue number reindexed from 1) K190 R226
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 HH2 A N11 R52 D84 N103 Q105 M128 D167 F172 A199 K203 R239 H241 N10 R39 D71 N90 Q92 M115 D154 F159 A186 K190 R226 H228
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
GO:0046677 response to antibiotic
Cellular Component
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1ad4, PDBe:1ad4, PDBj:1ad4
PDBsum1ad4
PubMed9149138
UniProtO05701|DHPS_STAAU Dihydropteroate synthase (Gene Name=folP)

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