Structure of PDB 6tho Chain B Binding Site BS02

Receptor Information
>6tho Chain B (length=219) Species: 103690 (Nostoc sp. PCC 7120 = FACHB-418) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HMQTLTLSPNLIGFNSNEGEKLLLTSRSREDFFPLSMQFVTQVNQAYCGV
ASIIMVLNSLGINAPETAQYSPYRVFTQDNFFSNEKTKAVIAPEVVARQG
MTLDELGRLIASYGVKVKVNHASDTNIEDFRKQVAENLKQDGNFVIVNYL
RKEIGQERGGHISPLAAYNEQTDRFLIMDVSRYKYPPVWVKTTDLWKAMN
TVDSVSQKTRGFVFVSKTQ
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 chain6tho Chain B Residue 1002 [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]
PDB6tho Structural and Biophysical Analysis of the Phytochelatin-Synthase-Like Enzyme from Nostoc sp. Shows That Its Protease Activity is Sensitive to the Redox State of the Substrate.
Resolution1.09 Å
Binding residue
(original residue number in PDB)
D30 N136 Q139 N142
Binding residue
(residue number reindexed from 1)
D31 N137 Q140 N143
Annotation score1
Enzymatic activity
Enzyme Commision number 2.3.2.15: glutathione gamma-glutamylcysteinyltransferase.
Gene Ontology
Molecular Function
GO:0016740 transferase activity
GO:0016756 glutathione gamma-glutamylcysteinyltransferase activity
GO:0046872 metal ion binding
Biological Process
GO:0010038 response to metal ion
GO:0046938 phytochelatin biosynthetic process

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:6tho, PDBe:6tho, PDBj:6tho
PDBsum6tho
PubMed35377603
UniProtQ8YY76

[Back to BioLiP]