Structure of PDB 1rvg Chain B Binding Site BS02

Receptor Information

>1rvg Chain B (length=305) Species: 271 (Thermus aquaticus)

MLVTGLEILKKAREEGYGVGAFNVNNMEFLQAVLEAAEEQRSPVILALSE
GAMKYGGRALTLMAVELAKEARVPVAVHLDHGSSYESVLRALRAGFTSVM
IDKSHEDFETNVRETRRVVEAAHAVGVTVEAELGRLAGIEEHVAVDEKDA
LLTNPEEARIFMERTGADYLAVAIGTSHGAYKGKGRPFIDHARLERIARL
VPAPLVLHGASAVPPELVERFRASGGEIGEAAGIHPEDIKKAISLGIAKI
NTDTDLRLAFTALIREALNKNPKEFDPRKYLGPAREAVKEVVKSRMELFG
SVGRA

Ligand information

• Ligand ID: SO4
• InChI: InChI=1S/H2O4S/c1-5(2,3)4/h(H2,1,2,3,4)/p-2
• InChIKey: QAOWNCQODCNURD-UHFFFAOYSA-L
• SMILES:
  OpenEye OEToolkits 1.5.0: [O-]S(=O)(=O)[O-]
  CACTVS 3.341: [O-][S]([O-])(=O)=O
  ACDLabs 10.04: [O-]S([O-])(=O)=O
• Formula: O4 S
• Name: SULFATE ION
• DrugBank: DB14546
• PDB chain: 1rvg Chain B Residue 1610

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1rvg Induced Fit Movements and Metal Cofactor Selectivity of Class II Aldolases: STRUCTURE OF THERMUS AQUATICUS FRUCTOSE-1,6-BISPHOSPHATE ALDOLASE.
• Resolution: 2.0 Å
• Binding residue (original residue number in PDB): R116 H123
• Binding residue (residue number reindexed from 1): R116 H123
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): D80 H81 E140 H178 H208 N251
• Catalytic site (residue number reindexed from 1): D80 H81 E140 H178 H208 N251
• Enzyme Commision number: 4.1.2.13: fructose-bisphosphate aldolase.

Gene Ontology

Molecular Function

• GO:0004332 fructose-bisphosphate aldolase activity
• GO:0008270 zinc ion binding
• GO:0016829 lyase activity
• GO:0016832 aldehyde-lyase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0005975 carbohydrate metabolic process
• GO:0006096 glycolytic process
• GO:0030388 fructose 1,6-bisphosphate metabolic process

External links

• PDB: RCSB:1rvg, PDBe:1rvg, PDBj:1rvg
• PDBsum: 1rvg
• PubMed: 14699122
• UniProt: Q9RHA2