Structure of PDB 1rvg Chain A Binding Site BS03

Receptor Information

>1rvg Chain A (length=299) Species: 271 (Thermus aquaticus)

MLVTGLEILKKAREEGYGVGAFNVNNMEFLQAVLEAAEEQRSPVILALSE
GAMKYGGRALTLMAVELAKEARVPVAVHLDHGSSYESVLRALRAGFTSVM
IDKSHEDFETNVRETRRVVEAAHAVGVTVEAELGRLAGIEEKDALLTNPE
EARIFMERTGADYLAVAIGTSHGAYKGKGRPFIDHARLERIARLVPAPLV
LHGASAVPPELVERFRASGGEIGEAAGIHPEDIKKAISLGIAKINTDTDL
RLAFTALIREALNKNPKEFDPRKYLGPAREAVKEVVKSRMELFGSVGRA

Ligand information

• Ligand ID: CO
• InChI: InChI=1S/Co/q+2
• InChIKey: XLJKHNWPARRRJB-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Co+2]
  CACTVS 3.341: [Co++]
• Formula: Co
• Name: COBALT (II) ION
• DrugBank: DB14205
• PDB chain: 1rvg Chain A Residue 1703

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): H81 H178 H208
• Binding residue (residue number reindexed from 1): H81 H172 H202
• 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 H172 H202 N245
• 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