Structure of PDB 1m0w Chain B

Receptor sequence
>1m0wB (length=479) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
PPSKDQLNELIQEVNQWAITNGLSMYPPKFEENPSNASVSPVTIYPTPIP
RKCFDEAVQIQPVFNELYARITQDMAQPDSYLHKTTEALALSDSEFTGKL
WSLYLATLKSAQYKKQNFRLGIFRSDYLIDKKKGTEQIKQVEFNTVSVSF
AGLSEKVDRLHSYLNRANKYDPKGPIYNDQNMVISDSGYLLSKALAKAVE
SYKSQQDPIVAFIVQRNERNVFDQKVLELNLLEKFGTKSVRLTFDDVNDK
LFIDDKTGKLFIRDTEQEIAVVYYRTGYTTTDYTSEKDWEARLFLEKSFA
IKAPDLLTQLSGSKKIQQLLTDEGVLGKYISDAEKKSSLLKTFVKIYPLD
DTKLGREGKRLALSEPSKYVLKPQREGNNVYKENIPNFLKGIEERHWDAY
ILMELIEPELNENNIILRDNKSYNEPIISELGIYGCVLFNDEQVLSNEFS
GSLLRSKFNTSNEGGVAAGFGCLDSIILY
3D structure
PDB1m0w Large Conformational Changes in the Catalytic Cycle of Glutathione Synthase
ChainB
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R1128 E1146 N1148 S1153 K1324 K1382 E1386 R1467
Catalytic site (residue number reindexed from 1) R124 E142 N144 S149 K314 K372 E376 R455
Enzyme Commision number 6.3.2.3: glutathione synthase.
Interaction with ligand
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004363 glutathione synthase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0042803 protein homodimerization activity
GO:0043295 glutathione binding
GO:0046872 metal ion binding
Biological Process
GO:0006750 glutathione biosynthetic process
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1m0w, PDBe:1m0w, PDBj:1m0w
PDBsum1m0w
PubMed12467574
UniProtQ08220|GSHB_YEAST Glutathione synthetase GSH2 (Gene Name=GSH2)

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