Structure of PDB 1v6d Chain A Binding Site BS03
Receptor Information
>1v6d Chain A (length=223) Species:
9823
(Sus scrofa) [
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IVGGYTCAANSIPYQVSLNSGSHFCGGSLINSQWVVSAAHCYKSRIQVRL
GEHNIDVLEGNEQFINAAKIITHPNFNGNTLDNDIMLIKLSSPATLNSRV
ATVSLPRSCAAAGTECLISGWGNTKSSGSSYPSLLQCLKAPVLSDSSCKS
SYPGQITGNMICVGFLEGGKDSCQGDSGGPVVCNGQLQGIVSWGYGCAQK
NKPGVYTKVCNYVNWIQQTIAAN
Ligand information
Ligand ID
ACT
InChI
InChI=1S/C2H4O2/c1-2(3)4/h1H3,(H,3,4)/p-1
InChIKey
QTBSBXVTEAMEQO-UHFFFAOYSA-M
SMILES
Software
SMILES
ACDLabs 10.04
[O-]C(=O)C
OpenEye OEToolkits 1.5.0
CC(=O)[O-]
CACTVS 3.341
CC([O-])=O
Formula
C2 H3 O2
Name
ACETATE ION
ChEMBL
DrugBank
DB14511
ZINC
PDB chain
1v6d Chain A Residue 390 [
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Receptor-Ligand Complex Structure
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PDB
1v6d
Secondary binding site of trypsin: revealed by crystal structure of trypsin-peptide complex.
Resolution
1.9 Å
Binding residue
(original residue number in PDB)
H57 Q192 G193 S195
Binding residue
(residue number reindexed from 1)
H40 Q174 G175 S177
Annotation score
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.
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:1v6d
,
PDBe:1v6d
,
PDBj:1v6d
PDBsum
1v6d
PubMed
15842169
UniProt
P00761
|TRYP_PIG Trypsin
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