Structure of PDB 2tbs Chain A

Receptor sequence
>2tbsA (length=222) Species: 8030 (Salmo salar) [Search protein sequence]
IVGGYECKAYSQAHQVSLNSGYHFCGGSLVNENWVVSAAHCYKSRVEVRL
GEHNIKVTEGSEQFISSSRVIRHPNYSSYNIDNDIMLIKLSKPATLNTYV
QPVALPTSCAPAGTMCTVSGWGNTMSSTADSDKLQCLNIPILSYSDCNDS
YPGMITNAMFCAGYLEGGKDSCQGDSGGPVVCNGELQGVVSWGYGCAEPG
NPGVYAKVCIFSDWLTSTMASY
3D structure
PDB2tbs Cold adaption of enzymes: structural comparison between salmon and bovine trypsins.
ChainA
Resolution1.8 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) H57 D102 Q192 G193 D194 S195 G196
Catalytic site (residue number reindexed from 1) H40 D84 Q173 G174 D175 S176 G177
Enzyme Commision number 3.4.21.4: trypsin.
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 A E70 N72 V75 E77 E80 E52 N54 V57 E59 E62
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
GO:0007586 digestion
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2tbs, PDBe:2tbs, PDBj:2tbs
PDBsum2tbs
PubMed7846025
UniProtP35031|TRY1_SALSA Trypsin-1

[Back to BioLiP]