Structure of PDB 1hj9 Chain A

Receptor sequence
>1hj9A (length=223) Species: 9913 (Bos taurus) [Search protein sequence]
IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRL
GEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRV
ASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKS
AYPGQITSNMFCAYGLEGKGDSCQGDSGGPVVCSGKLQGIVSWGSGCQAK
NKPGVYTKVCNYVSWIKQTIASN
3D structure
PDB1hj9 Atomic Resolution Structure of Trypsin Provide Insight Into Structural Radiation Damage
ChainA
Resolution0.95 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 Q174 G175 D176 S177 G178
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 ANL A S190 V213 S172 V191
BS02 CA A E70 N72 V75 E80 E52 N54 V57 E62
Gene Ontology
Molecular Function
GO:0004175 endopeptidase activity
GO:0004252 serine-type endopeptidase activity
GO:0005515 protein binding
GO:0008236 serine-type peptidase activity
GO:0046872 metal ion binding
GO:0097655 serpin family protein binding
Biological Process
GO:0006508 proteolysis
GO:0007586 digestion
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space
GO:0097180 serine protease inhibitor complex

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1hj9, PDBe:1hj9, PDBj:1hj9
PDBsum1hj9
PubMed11264577
UniProtP00760|TRY1_BOVIN Serine protease 1 (Gene Name=PRSS1)

[Back to BioLiP]