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Structure of PDB 2a31 Chain A

Receptor sequence >2a31A (length=223) Species: 9823 (Sus scrofa) [Search protein sequence] IVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRL GEHNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRV ATVSLPRSCAAAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSDSSCKS SYPGQITGNMICVGFLEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCAQK NKPGVYTKVCNYVNWIQQTIAAN

3D structure PDB 2a31 NMR and crystallographic characterization of adventitious borate binding by trypsin. Chain A Resolution 1.25 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 CA A E70 N72 V75 L76 E80 E52 N54 V57 L58 E62 BS02 MG A E70 N72 V75 E80 E52 N54 V57 E62 BS03 BO4 A S164 S167 S144 S147 BS04 PG3 A D189 S190 C191 S195 V213 S214 W215 G216 D171 S172 C173 S177 V191 S192 W193 G194

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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