Structure of PDB 1gyn Chain A Binding Site BS02

Receptor Information

>1gyn Chain A (length=333) Species: 562 (Escherichia coli)

SKIFDFVKPGVITGDDVQKVFQVAKENNFALPAVNCVGTDSINAVLETAA
KVKAPVIVQFSNGGASFIAGKGVKSDVPQGAAILGAISGAHHVHQMAEHY
GVPVILHTDHCAKKLLPWIDGLLDAGEKHFAATGKPLFSSHMIDLSEESL
QENIEICSKYLERMSKIGMTLEIELGALYTQPEDVDYAYTELSKISPRFT
IAASFGNVVVLTPTILRDSQEYVSKKHNLPHNSLNFVFHGGSGSTAQEIK
DSVSYGVVKMNIDTDTQWATWEGVLNYYKANEAYLQGQLGNPKGEDQPNK
KYYDPRVWLRAGQTSMIARLEKAFQELNAIDVL

Ligand information

• Ligand ID: CD
• InChI: InChI=1S/Cd/q+2
• InChIKey: WLZRMCYVCSSEQC-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Cd++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Cd+2]
• Formula: Cd
• Name: CADMIUM ION
• PDB chain: 1gyn Chain A Residue 402

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1gyn The Organization of Divalent Cations in the Active Site of Cadmium Escherichia Coli Fructose 1,6-Bisphosphate Aldolase
• Resolution: 2.0 Å
• Binding residue (original residue number in PDB): D144 E174
• Binding residue (residue number reindexed from 1): D144 E174
• Annotation score: 1

Enzymatic activity

• Catalytic site (original residue number in PDB): D109 H110 H264 N286
• Catalytic site (residue number reindexed from 1): D109 H110 H239 N261
• Enzyme Commision number: 4.1.2.13: fructose-bisphosphate aldolase.

Gene Ontology

Molecular Function

• GO:0004332 fructose-bisphosphate aldolase activity
• GO:0005515 protein binding
• GO:0008270 zinc ion binding
• GO:0016829 lyase activity
• GO:0016832 aldehyde-lyase activity
• GO:0042802 identical protein binding
• GO:0042803 protein homodimerization activity
• GO:0046872 metal ion binding

Biological Process

• GO:0005975 carbohydrate metabolic process
• GO:0006094 gluconeogenesis
• GO:0006096 glycolytic process

Cellular Component

• GO:0005829 cytosol

External links

• PDB: RCSB:1gyn, PDBe:1gyn, PDBj:1gyn
• PDBsum: 1gyn
• PubMed: 12595741
• UniProt: P0AB71|ALF_ECOLI Fructose-bisphosphate aldolase class 2 (Gene Name=fbaA)