Structure of PDB 1s6f Chain A

Receptor sequence
>1s6fA (length=223) Species: 9823 (Sus scrofa) [Search protein sequence]
IVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRL
GEHNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRV
ATVSLPRSCAAAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSDSSCKS
SYPGQITGNMICVGFLEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCAQK
NKPGVYTKVCNYVNWIQQTIAAN
3D structure
PDB1s6f X-ray and NMR characterization of covalent complexes of trypsin, borate, and alcohols.
ChainA
Resolution1.8 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 CA A E70 N72 V75 L76 E80 E52 N54 V57 L58 E62
BS02 SBP A H57 D189 S190 C191 G193 S195 G216 H40 D171 S172 C173 G175 S177 G194
BS03 EDO A S39 H40 I73 S22 H23 I55
BS04 EDO A S164 S166 S144 S146
BS05 EDO A N48 Q239 N31 Q217
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

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Cellular Component
External links
PDB RCSB:1s6f, PDBe:1s6f, PDBj:1s6f
PDBsum1s6f
PubMed15005618
UniProtP00761|TRYP_PIG Trypsin

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