Structure of PDB 1slx Chain B Binding Site BS02
Receptor Information
>1slx Chain B (length=219) Species:
10116
(Rattus norvegicus) [
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IVGGYTCQENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRL
GEHNINVLEGNEQFVNAAKIIKHPNFDRKTLNNDIMLIKLSSPVKVATVA
LPSSCAPAGTQCLISGWGHTLSSGVNHPDLLQCLDAPLLPQADCEASYPG
KITDNMVCVGFLEGGKDSCQGDSGGPVVCNGELQGIVSWGYGCALPDNPG
VYTKVCNYVDWIQDTIAAN
Ligand information
Ligand ID
ZN
InChI
InChI=1S/Zn/q+2
InChIKey
PTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
Software
SMILES
CACTVS 3.341
[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Zn+2]
Formula
Zn
Name
ZINC ION
ChEMBL
CHEMBL1236970
DrugBank
DB14532
ZINC
PDB chain
1slx Chain B Residue 248 [
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Receptor-Ligand Complex Structure
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PDB
1slx
X-ray structures of a designed binding site in trypsin show metal-dependent geometry.
Resolution
2.2 Å
Binding residue
(original residue number in PDB)
H143 H151
Binding residue
(residue number reindexed from 1)
H119 H127
Annotation score
4
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 Q170 G171 D172 S173 G174
Enzyme Commision number
3.4.21.4
: trypsin.
Gene Ontology
Molecular Function
GO:0004252
serine-type endopeptidase activity
GO:0005509
calcium ion binding
GO:0005515
protein binding
GO:0008236
serine-type peptidase activity
GO:0046872
metal ion binding
Biological Process
GO:0006508
proteolysis
GO:0007584
response to nutrient
GO:0007586
digestion
GO:0030574
collagen catabolic process
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:1slx
,
PDBe:1slx
,
PDBj:1slx
PDBsum
1slx
PubMed
8634241
UniProt
P00763
|TRY2_RAT Anionic trypsin-2 (Gene Name=Prss2)
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