Structure of PDB 6tho Chain A

Receptor sequence
>6thoA (length=220) Species: 103690 (Nostoc sp. PCC 7120 = FACHB-418) [Search protein sequence]
GPHMQTLTLSPNLIGFNSNEGEKLLLTSRSREDFFPLSMQFVTQVNQAYC
GVASIIMVLNSLGINAPETAQYSPYRVFTQDNFFSNEKTKAVIAPEVVAR
QGMTLDELGRLIASYGVKVKVNHASDTNIEDFRKQVAENLKQDGNFVIVN
YLRKEIGQERGGHISPLAAYNEQTDRFLIMDVSRYKYPPVWVKTTDLWKA
MNTVDSVSQKTRGFVFVSKT
3D structure
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.
ChainA
Resolution1.09 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.3.2.15: glutathione gamma-glutamylcysteinyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 GDS A Q44 A45 C47 R97 Q98 G99 M100 G159 D202 R209 Q47 A48 C50 R100 Q101 G102 M103 G162 D205 R212
BS02 CA A D30 N136 Q139 N142 D33 N139 Q142 N145
BS03 CA A E29 D140 E32 D143
BS04 CA A N16 E19 N19 E22
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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