Structure of PDB 5u12 Chain A

Receptor sequence
>5u12A (length=264) Species: 199310 (Escherichia coli CFT073) [Search protein sequence]
SMKLFAQGTSLDLSHPHVMGILNVTNSLIDAVKHANLMINAGATIIDVGG
ESTRPGAAEVSVEEELQRVIPVVEAIAQRFEVWISVDTSKPEVIRESAKV
GAHIINDIRSLSEPGALEAAAETGLPVCLMHMQPKYDDVFAEVNRYFIEQ
IARCEQAGIAKEKLLLDPGFGFGKNLSHNYSLLARLAEFHHFNLPLLVGM
SRKSMIGQLLNVGPSERLSGSLACAVIAAMQGAHIIRVHDVKETVEAMRV
VEATLSAKENKRYE
3D structure
PDB5u12 8-Mercaptoguanine Derivatives as Inhibitors of Dihydropteroate Synthase.
ChainA
Resolution1.839 Å
3D
structure
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Enzymatic activity
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 5RU A T62 N115 M139 D185 F190 G217 K221 R255 T53 N106 M130 D167 F172 G199 K203 R237 PDBbind-CN: -logKd/Ki=5.07,Kd=8.5uM
BindingDB: Kd=8500nM
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:5u12, PDBe:5u12, PDBj:5u12
PDBsum5u12
PubMed29171692
UniProtP0AC13|DHPS_ECOLI Dihydropteroate synthase (Gene Name=folP)

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