Structure of PDB 1fmg Chain A

Receptor sequence
>1fmgA (length=223) Species: 9823 (Sus scrofa) [Search protein sequence]
IVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRL
GEHNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRV
ATVSLPRSCAAAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSNSSCKS
SYPGQITGNMICVGFLQGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCAQK
NKPGVYTKVCNYVNWIQQTIAAN
3D structure
PDB1fmg Structures of porcine beta-trypsin-detergent complexes: the stabilization of proteins through hydrophilic binding of polydocanol.
ChainA
Resolution1.9 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 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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1fmg, PDBe:1fmg, PDBj:1fmg
PDBsum1fmg
PubMed11679713
UniProtP00761|TRYP_PIG Trypsin

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