Structure of PDB 3tyd Chain A Binding Site BS01

Receptor Information

>3tyd Chain A (length=271) Species: 191218 (Bacillus anthracis str. A2012)

KWDYDLRCGEYTLNLNEKTLIMGILNVTPDSFSGSYNEVDAAVRHAKEMR
DEGAHIIDIGGESTRPGFAKVSVEEEIKRVVPMIQAVSKEVKLPISIDTY
KAEVAKQAIEAGAHIINDIWGAKAEPKIAEVAAHYDVPIILMHNRDNMNY
RNLMADMIADLYDSIKIAKDAGVRDENIILDPGIGFAKTPEQNLEAMRNL
EQLNVLGYPVLLGTSRKSFIGHVLDLPVEERLEGTGATVCLGIEKGCEFV
RVHDVKEMSRMAKMMDAMIGK

Ligand information

• Ligand ID: POP
• InChI: InChI=1S/H4O7P2/c1-8(2,3)7-9(4,5)6/h(H2,1,2,3)(H2,4,5,6)/p-2
• InChIKey: XPPKVPWEQAFLFU-UHFFFAOYSA-L
• SMILES:
  OpenEye OEToolkits 1.5.0: O[P@@](=O)([O-])O[P@@](=O)(O)[O-]
  CACTVS 3.341: O[P]([O-])(=O)O[P](O)([O-])=O
  ACDLabs 10.04: [O-]P(=O)(O)OP([O-])(=O)O
  OpenEye OEToolkits 1.5.0: OP(=O)([O-])OP(=O)(O)[O-]
• Formula: H2 O7 P2
• Name: PYROPHOSPHATE 2-
• PDB chain: 3tyd Chain A Residue 701

Receptor-Ligand Complex Structure

Structure summary

• PDB: 3tyd Catalysis and sulfa drug resistance in dihydropteroate synthase.
• Resolution: 2.5 Å
• Binding residue (original residue number in PDB): N27 S66 R254 H256
• Binding residue (residue number reindexed from 1): N26 S63 R251 H253
• Annotation score: 5

Enzymatic activity

• Catalytic site (original residue number in PDB): V28 D54 K220 R254
• Catalytic site (residue number reindexed from 1): V27 D51 K217 R251
• 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:3tyd, PDBe:3tyd, PDBj:3tyd
• PDBsum: 3tyd
• PubMed: 22383850
• UniProt: Q81VW8