Structure of PDB 3tyu Chain B

Receptor sequence
>3tyuB (length=238) Species: 632 (Yersinia pestis) [Search protein sequence]
SHMHLTARGLTLDLSRPQVMGILNNNLDQALQHAQRMLSAGATLIDIGEL
DRVVPVVEALAQRFDVWLSVDTSKAAVITESAHAGAHLINDIRSLQEPGA
LEAAAKTGLPVCLMHMQDLMTDINRFFQHHIERCVAAGIAKNKLLLDPGF
GFGKNLAHNYQLLAHLSELHHFELPLLVGMSRKSMVGQLLNVPPQQRVIG
SVACAVIAAMQGAQIIRVHDVKETVEAMCIVEATRSAK
3D structure
PDB3tyu Catalysis and sulfa drug resistance in dihydropteroate synthase.
ChainB
Resolution2.7 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) K183 R217
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 PT1 B N115 D185 G189 F190 K221 S222 R255 N90 D147 G151 F152 K183 S184 R217
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
Cellular Component
GO:0005829 cytosol

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Cellular Component
External links
PDB RCSB:3tyu, PDBe:3tyu, PDBj:3tyu
PDBsum3tyu
PubMed22383850
UniProtA0A2S9PLG4

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