Structure of PDB 6tho Chain B Binding Site BS01

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 IDGDS
InChIInChI=1S/C20H32N6O12S2/c21-9(19(35)36)1-3-13(27)25-11(17(33)23-5-15(29)30)7-39-40-8-12(18(34)24-6-16(31)32)26-14(28)4-2-10(22)20(37)38/h9-12H,1-8,21-22H2,(H,23,33)(H,24,34)(H,25,27)(H,26,28)(H,29,30)(H,31,32)(H,35,36)(H,37,38)/t9-,10-,11-,12-/m0/s1
InChIKeyYPZRWBKMTBYPTK-BJDJZHNGSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(CC(=O)N[C@@H](CSSC[C@@H](C(=O)NCC(=O)O)NC(=O)CC[C@@H](C(=O)O)N)C(=O)NCC(=O)O)[C@@H](C(=O)O)N
CACTVS 3.341N[CH](CCC(=O)N[CH](CSSC[CH](NC(=O)CC[CH](N)C(O)=O)C(=O)NCC(O)=O)C(=O)NCC(O)=O)C(O)=O
CACTVS 3.341N[C@@H](CCC(=O)N[C@@H](CSSC[C@H](NC(=O)CC[C@H](N)C(O)=O)C(=O)NCC(O)=O)C(=O)NCC(O)=O)C(O)=O
OpenEye OEToolkits 1.5.0C(CC(=O)NC(CSSCC(C(=O)NCC(=O)O)NC(=O)CCC(C(=O)O)N)C(=O)NCC(=O)O)C(C(=O)O)N
ACDLabs 10.04O=C(NC(C(=O)NCC(=O)O)CSSCC(C(=O)NCC(=O)O)NC(=O)CCC(C(=O)O)N)CCC(C(=O)O)N
FormulaC20 H32 N6 O12 S2
NameOXIDIZED GLUTATHIONE DISULFIDE
ChEMBLCHEMBL1372
DrugBankDB03310
ZINCZINC000003870129
PDB chain6tho Chain B Residue 1001 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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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)		Q44 A45 C47 R97 Q98 G99 M100 G159 D202 R209
Binding residue
(residue number reindexed from 1)		Q45 A46 C48 R98 Q99 G100 M101 G160 D203 R210
Annotation score3
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

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