Structure of PDB 1aq7 Chain A

Receptor sequence
>1aq7A (length=223) Species: 9913 (Bos taurus) [Search protein sequence]
IVGGYTCGANTVPYQVSLNSGYHFCGGSLINSQWVVSAAHCYKSGIQVRL
GEDNINVVEGNEQFISASKSIVHPSYNSNTLNNDIMLIKLKSAASLNSRV
ASISLPTSCASAGTQCLISGWGNTKSSGTSYPDVLKCLKAPILSDSSCKS
AYPGQITSNMFCAGYLEGGKDSCQGDSGGPVVCSGKLQGIVSWGSGCAQK
NKPGVYTKVCNYVSWIKQTIASN
3D structure
PDB1aq7 Aeruginosins 98-A and B, Trypsin Inhibitors from the Blue-Green Alga Microcystis Aeruginosa (Nies-98)
ChainA
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) 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 peptide A H57 L99 D189 S190 C191 Q192 S214 W215 G216 G219 C220 G226 H40 L81 D171 S172 C173 Q174 S192 W193 G194 G196 C197 G204
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1aq7, PDBe:1aq7, PDBj:1aq7
PDBsum1aq7
PubMed
UniProtP00760|TRY1_BOVIN Serine protease 1 (Gene Name=PRSS1)

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