Structure of PDB 2tec Chain E

Receptor sequence
>2tecE (length=279) Species: 2026 (Thermoactinomyces vulgaris) [Search protein sequence]
YTPNDPYFSSRQYGPQKIQAPQAWDIAEGSGAKIAIVDTGVQSNHPDLAG
KVVGGWDFVDNDSTPQNGNGHGTHCAGIAAAVTNNSTGIAGTAPKASILA
VRVLDNSGSGTWTAVANGITYAADQGAKVISLSLGGTVGNSGLQQAVNYA
WNKGSVVVAAAGNAGNTAPNYPAYYSNAIAVASTDQNDNKSSFSTYGSVV
DVAAPGSWIYSTYPTSTYASLSGTSMATPHVAGVAGLLASQGRSASNIRA
AIENTADKISGTGTYWAKGRVNAYKAVQY
3D structure
PDB2tec 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.
ChainE
Resolution1.98 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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
BS03 CA E A173 Y174 Y175 A178 A173 Y174 Y175 A178
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2tec, PDBe:2tec, PDBj:2tec
PDBsum2tec
PubMed2689655
UniProtP04072|THET_THEVU Thermitase

[Back to BioLiP]