Structure of PDB 6tho Chain A Binding Site BS04

Receptor Information
>6tho Chain A (length=220) 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]
GPHMQTLTLSPNLIGFNSNEGEKLLLTSRSREDFFPLSMQFVTQVNQAYC
GVASIIMVLNSLGINAPETAQYSPYRVFTQDNFFSNEKTKAVIAPEVVAR
QGMTLDELGRLIASYGVKVKVNHASDTNIEDFRKQVAENLKQDGNFVIVN
YLRKEIGQERGGHISPLAAYNEQTDRFLIMDVSRYKYPPVWVKTTDLWKA
MNTVDSVSQKTRGFVFVSKT
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 A Residue 1004 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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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)		N16 E19
Binding residue
(residue number reindexed from 1)		N19 E22
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

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Molecular Function
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Biological Process
External links
PDB RCSB:6tho, PDBe:6tho, PDBj:6tho
PDBsum6tho
PubMed35377603
UniProtQ8YY76

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