Structure of PDB 1mct Chain A Binding Site BS01
Receptor Information
>1mct Chain A (length=223) Species:
9823
(Sus scrofa) [
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IVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRL
GEHNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRV
ATVSLPRSCAAAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSNSSCKS
SYPGQITGNMICVGFLQGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCAQK
NKPGVYTKVCNYVNWIQQTIAAN
Ligand information
>1mct Chain I (length=28) Species:
3673
(Momordica charantia) [
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RICPRIWMECTRDSDCMAKCICVAGHCG
Receptor-Ligand Complex Structure
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PDB
1mct
Refined 1.6 A resolution crystal structure of the complex formed between porcine beta-trypsin and MCTI-A, a trypsin inhibitor of the squash family. Detailed comparison with bovine beta-trypsin and its complex.
Resolution
1.6 Å
Binding residue
(original residue number in PDB)
F41 H57 L99 Y151 Q175 D189 S190 C191 Q192 G193 S195 S214 W215 G216 Y217
Binding residue
(residue number reindexed from 1)
F24 H40 L81 Y131 Q155 D171 S172 C173 Q174 G175 S177 S192 W193 G194 Y195
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.
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:1mct
,
PDBe:1mct
,
PDBj:1mct
PDBsum
1mct
PubMed
8445634
UniProt
P00761
|TRYP_PIG Trypsin
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