Structure of PDB 2a32 Chain A

Receptor sequence
>2a32A (length=223) Species: 9823 (Sus scrofa) [Search protein sequence]
IVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRL
GEHNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRV
ATVSLPRSCAAAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSDSSCKS
SYPGQITGNMICVGFLEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCAQK
NKPGVYTKVCNYVNWIQQTIAAN
3D structure
PDB2a32 NMR and crystallographic characterization of adventitious borate binding by trypsin.
ChainA
Resolution1.5 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 E80 E52 N54 V57 E62
BS02 PG3 A D189 S190 C191 Q192 G219 C220 D171 S172 C173 Q174 G196 C197
BS03 PBC A H57 Q192 S195 H40 Q174 S177
BS04 PBC A S164 S167 S144 S147
BS05 BO4 A S164 S167 S144 S147
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:2a32, PDBe:2a32, PDBj:2a32
PDBsum2a32
PubMed16536459
UniProtP00761|TRYP_PIG Trypsin

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