Structure of PDB 5v79 Chain A

Receptor sequence
>5v79A (length=266) Species: 199310 (Escherichia coli CFT073) [Search protein sequence]
MKLFAQGTSLDLSHPHVMGILNVTNSLIDAVKHANLMINAGATIIDVGGE
STRPGAAEVSVEEELQRVIPVVEAIAQRFEVWISVDTSKPEVIRESAKVG
AHIINDIRSLSEPGALEAAAETGLPVCLMHMQGNPKTMQEAPKYDDVFAE
VNRYFIEQIARCEQAGIAKEKLLLDPGFGFGKNLSHNYSLLARLAEFHHF
NLPLLVGMSRKSMIGQLLNVGPSERLSGSLACAVIAAMQGAHIIRVHDVK
ETVEAMRVVEATLSAK
3D structure
PDB5v79 8-Mercaptoguanine Derivatives as Inhibitors of Dihydropteroate Synthase.
ChainA
Resolution2.25 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 8Y4 A T62 D96 N115 M139 D185 F190 G217 R220 K221 R255 H257 T52 D86 N105 M129 D175 F180 G207 R210 K211 R245 H247 PDBbind-CN: -logKd/Ki=6.41,Kd=0.39uM
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:5v79, PDBe:5v79, PDBj:5v79
PDBsum5v79
PubMed29171692
UniProtP0AC13|DHPS_ECOLI Dihydropteroate synthase (Gene Name=folP)

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