Structure of PDB 1tec Chain E

Receptor sequence
>1tecE (length=279) Species: 2026 (Thermoactinomyces vulgaris) [Search protein sequence]
YTPNDPYFSSRQYGPQKIQAPQAWDIAEGSGAKIAIVDTGVQSNHPDLAG
KVVGGWDFVDNDSTPQNGNGHGTHCAGIAAAVTNNSTGIAGTAPKASILA
VRVLDNSGSGTWTAVANGITYAADQGAKVISLSLGGTVGNSGLQQAVNYA
WNKGSVVVAAAGNAGNTAPNYPAYYSNAIAVASTDQNDNKSSFSTYGSVV
DVAAPGSWIYSTYPTSTYASLSGTSMATPHVAGVAGLLASQGRSASNIRA
AIENTADKISGTGTYWAKGRVNAYKAVQY
3D structure
PDB1tec Crystallographic refinement by incorporation of molecular dynamics: thermostable serine protease thermitase complexed with eglin c.
ChainE
Resolution2.2 Å
3D
structure
Catalytic site residues are labeled in the structure
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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.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 CA E D5 D47 V82 N85 T87 I89 D5 D47 V82 N85 T87 I89
BS02 CA E D57 D60 D62 T64 Q66 D57 D60 D62 T64 Q66
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

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Cellular Component
External links
PDB RCSB:1tec, PDBe:1tec, PDBj:1tec
PDBsum1tec
PubMed2688688
UniProtP04072|THET_THEVU Thermitase

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