Structure of PDB 5u14 Chain A

Receptor sequence
>5u14A (length=273) Species: 199310 (Escherichia coli CFT073) [Search protein sequence]
MKLFAQGTSLDLSHPHVMGILNVTPNSLIDAVKHANLMINAGATIIDVGG
ESTRPGAAEVSVEEELQRVIPVVEAIAQRFEVWISVDTSKPEVIRESAKV
GAHIINDIRSLSEPGALEAAAETGLPVCLMHMQGNPKTMQEAPKYDDVFA
EVNRYFIEQIARCEQAGIAKEKLLLDPGFGFGKNLSHNYSLLARLAEFHH
FNLPLLVGMSRKSMIGQLLNVGPSERLSGSLACAVIAAMQGAHIIRVHDV
KETVEAMRVVEATLSAKENKRYE
3D structure
PDB5u14 8-Mercaptoguanine Derivatives as Inhibitors of Dihydropteroate Synthase.
ChainA
Resolution1.953 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 7PV A T62 R63 P64 N115 I117 M139 D185 F190 G217 K221 S222 R255 T53 R54 P55 N106 I108 M130 D176 F181 G208 K212 S213 R246 PDBbind-CN: -logKd/Ki=5.34,Kd=4.6uM
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:5u14, PDBe:5u14, PDBj:5u14
PDBsum5u14
PubMed29171692
UniProtP0AC13|DHPS_ECOLI Dihydropteroate synthase (Gene Name=folP)

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