Structure of PDB 2tec Chain E Binding Site BS02

Receptor Information

>2tec Chain E (length=279) Species: 2026 (Thermoactinomyces vulgaris)

YTPNDPYFSSRQYGPQKIQAPQAWDIAEGSGAKIAIVDTGVQSNHPDLAG
KVVGGWDFVDNDSTPQNGNGHGTHCAGIAAAVTNNSTGIAGTAPKASILA
VRVLDNSGSGTWTAVANGITYAADQGAKVISLSLGGTVGNSGLQQAVNYA
WNKGSVVVAAAGNAGNTAPNYPAYYSNAIAVASTDQNDNKSSFSTYGSVV
DVAAPGSWIYSTYPTSTYASLSGTSMATPHVAGVAGLLASQGRSASNIRA
AIENTADKISGTGTYWAKGRVNAYKAVQY

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: 2tec Chain E Residue 344

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2tec Molecular dynamics refinement of a thermitase-eglin-c complex at 1.98 A resolution and comparison of two crystal forms that differ in calcium content.
• Resolution: 1.98 Å
• Binding residue (original residue number in PDB): D57 D60 D62 T64 Q66
• Binding residue (residue number reindexed from 1): D57 D60 D62 T64 Q66
• Annotation score: 4

Enzymatic activity

• Catalytic site (original residue number in PDB): S225
• Catalytic site (residue number reindexed from 1): S225
• Enzyme Commision number: 3.4.21.66: thermitase.

Gene Ontology

Molecular Function

• GO:0004252 serine-type endopeptidase activity
• GO:0008236 serine-type peptidase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0006508 proteolysis

Cellular Component

• GO:0005576 extracellular region

External links

• PDB: RCSB:2tec, PDBe:2tec, PDBj:2tec
• PDBsum: 2tec
• PubMed: 2689655
• UniProt: P04072|THET_THEVU Thermitase