Structure of PDB 1aj0 Chain A

Receptor sequence
>1aj0A (length=282) Species: 562 (Escherichia coli) [Search protein sequence]
MKLFAQGTSLDLSHPHVMGILNVTPDSFSDGGTHNSLIDAVKHANLMINA
GATIIDVGGESTRPGAAEVSVEEELQRVIPVVEAIAQRFEVWISVDTSKP
EVIRESAKVGAHIINDIRSLSEPGALEAAAETGLPVCLMHMQGNPKTMQE
APKYDDVFAEVNRYFIEQIARCEQAGIAKEKLLLDPGFGFGKNLSHNYSL
LARLAEFHHFNLPLLVGMSRKSMIGQLLNVGPSERLSGSLACAVIAAMQG
AHIIRVHDVKETVEAMRVVEATLSAKENKRYE
3D structure
PDB1aj0 Crystal structure of the anti-bacterial sulfonamide drug target dihydropteroate synthase.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K221 R255
Catalytic site (residue number reindexed from 1) K221 R255
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 PH2 A T62 N115 I117 M139 D185 F190 K221 R255 T62 N115 I117 M139 D185 F190 K221 R255
BS02 SAN A R63 S219 R220 K221 R63 S219 R220 K221
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:0009410 response to xenobiotic stimulus
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:0005737 cytoplasm
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:1aj0, PDBe:1aj0, PDBj:1aj0
PDBsum1aj0
PubMed9187658
UniProtP0AC13|DHPS_ECOLI Dihydropteroate synthase (Gene Name=folP)

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