Structure of PDB 1amh Chain B Binding Site BS01

Receptor Information
>1amh Chain B (length=223) Species: 10117 (Rattus rattus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
IVGGYTCQENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRL
GEHNINVLEGNEQFVNAAKIIKHPNFDRKTLNNDIMLIKLSSPVKLNARV
ATVALPSSCAPAGTQCLISGWGNTLSSGVNEPDLLQCLDAPLLPQADCEA
SYPGKITDNMVCVGFLEGGKSSCQGDSGGPVVCNGELQGIVSWGYGCALP
DNPGVYTKVCNYVDWIQDTIAAN
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain1amh Chain B Residue 246 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB1amh The three-dimensional structure of Asp189Ser trypsin provides evidence for an inherent structural plasticity of the protease.
Resolution2.5 Å
Binding residue
(original residue number in PDB)		E70 N72 V75 E77 E80
Binding residue
(residue number reindexed from 1)		E52 N54 V57 E59 E62
Annotation score4
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: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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1amh, PDBe:1amh, PDBj:1amh
PDBsum1amh
PubMed10429182
UniProtP00763|TRY2_RAT Anionic trypsin-2 (Gene Name=Prss2)

[Back to BioLiP]