Structure of PDB 3tzf Chain A

Receptor sequence
>3tzfA (length=275) Species: 632 (Yersinia pestis) [Search protein sequence]
MHLTARGLTLDLSRPQVMGILNVTPDSFSDGGCHNNLDQALQHAQRMLSA
GATLIDIGGESTRPGAAEVSEQEELDRVVPVVEALAQRFDVWLSVDTSKA
AVITESAHAGAHLINDIRSLQEPGALEAAAKTGLPVCLMHMQGQPKNMQH
SPYYDDLMTDINRFFQHHIERCVAAGIAKNKLLLDPGFGFGKNLAHNYQL
LAHLSELHHFELPLLVGMSRKSMVGQLLNVPPQQRVIGSVACAVIAAMQG
AQIIRVHDVKETVEAMCIVEATRSA
3D structure
PDB3tzf Catalysis and sulfa drug resistance in dihydropteroate synthase.
ChainA
Resolution2.1 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 HH2 A N22 S27 F28 S61 T62 D96 N115 I117 M139 D185 F190 G217 K221 R255 H257 N22 S27 F28 S61 T62 D96 N115 I117 M139 D185 F190 G217 K221 R255 H257
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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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3tzf, PDBe:3tzf, PDBj:3tzf
PDBsum3tzf
PubMed22383850
UniProtA0A2S9PLG4

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