Structure of PDB 3tyz Chain B Binding Site BS03

Receptor Information

>3tyz Chain B (length=276) Species: 632 (Yersinia pestis)

MHLTARGLTLDLSRPQVMGILNVTPDSFSDGGCHNNLDQALQHAQRMLSA
GATLIDIGGESTRPGAAEVSEQEELDRVVPVVEALAQRFDVWLSVDTSKA
AVITESAHAGAHLINDIRSLQEPGALEAAAKTGLPVCLMHMQGQPKNMQH
SPYYDDLMTDINRFFQHHIERCVAAGIAKNKLLLDPGFGFGKNLAHNYQL
LAHLSELHHFELPLLVGMSRKSMVGQLLNVPPQQRVIGSVACAVIAAMQG
AQIIRVHDVKETVEAMCIVEATRSAK

Ligand information

• Ligand ID: PAB
• InChI: InChI=1S/C7H7NO2/c8-6-3-1-5(2-4-6)7(9)10/h1-4H,8H2,(H,9,10)
• InChIKey: ALYNCZNDIQEVRV-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: Nc1ccc(cc1)C(O)=O
  ACDLabs 10.04: O=C(O)c1ccc(N)cc1
  OpenEye OEToolkits 1.5.0: c1cc(ccc1C(=O)O)N
• Formula: C7 H7 N O2
• Name: 4-AMINOBENZOIC ACID
• ChEMBL: CHEMBL542
• DrugBank: DB02362
• ZINC: ZINC000000000920
• PDB chain: 3tyz Chain B Residue 280

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3tyz Catalysis and sulfa drug resistance in dihydropteroate synthase.
• Resolution: 2.07 Å
• Binding residue (original residue number in PDB): F28 T62 R63 G189 F190 K221 S222
• Binding residue (residue number reindexed from 1): F28 T62 R63 G189 F190 K221 S222
• Annotation score: 5

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.

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

External links

• PDB: RCSB:3tyz, PDBe:3tyz, PDBj:3tyz
• PDBsum: 3tyz
• PubMed: 22383850
• UniProt: A0A2S9PLG4