Structure of PDB 1qi3 Chain A Binding Site BS06

Receptor Information

>1qi3 Chain A (length=418) Species: 316 (Stutzerimonas stutzeri)

DQAGKSPNAVRYHGGDEIILQGFHWNVVREAPNDWYNILRQQAATIAADG
FSAIWMPVPWRDFSSWSDGSKSGGGEGYFWHDFNKNGRYGSDAQLRQAAS
ALGGAGVKVLYDVVPNHMNRGYPDKEINLPAGQGFWRNDCADPGNYPNDC
DDGDRFIGGDADLNTGHPQVYGMFRDEFTNLRSQYGAGGFRFNFVRGYAP
ERVNSWMTDSADNSFCVGELWKGPSEYPNWDWRNTASWQQIIKDWSDRAK
CPVFDFALKERMQNGSIADWKHGLNGNPDPRWREVAVTFVDNHDTGYSPG
QNGGQHHWALQDGLIRQAYAYILTSPGTPVVYWDHMYDWGYGDFIRQLIQ
VRRAAGVRADSAISFHSGYSGLVATVSGSQQTLVVALNSDLGNPGQVASG
SFSEAVNASNGQVRVWRS

Ligand information

• Ligand ID: CA
• InChI: InChI=1S/Ca/q+2
• InChIKey: BHPQYMZQTOCNFJ-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Ca++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Ca+2]
• Formula: Ca
• Name: CALCIUM ION
• DrugBank: DB14577
• PDB chain: 1qi3 Chain A Residue 452

Receptor-Ligand Complex Structure

Structure summary

• PDB: 1qi3 Roles of catalytic residues in alpha-amylases as evidenced by the structures of the product-complexed mutants of a maltotetraose-forming amylase.
• Resolution: 2.0 Å
• Binding residue (original residue number in PDB): D1 Q2 H13 D16 E17
• Binding residue (residue number reindexed from 1): D1 Q2 H13 D16 E17
• Annotation score: 4

Enzymatic activity

• Catalytic site (original residue number in PDB): N193 E219 D294
• Catalytic site (residue number reindexed from 1): N193 E219 D294
• Enzyme Commision number: 3.2.1.60: glucan 1,4-alpha-maltotetraohydrolase.

Gene Ontology

Biological Process

• GO:0005975 carbohydrate metabolic process

External links

• PDB: RCSB:1qi3, PDBe:1qi3, PDBj:1qi3
• PDBsum: 1qi3
• PubMed: 10556241
• UniProt: P13507|AMT4_STUST Glucan 1,4-alpha-maltotetraohydrolase (Gene Name=amyP)