Structure of PDB 1m0w Chain A

Receptor sequence
>1m0wA (length=481) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
PSKDQLNELIQEVNQWAITNGLSMYPPKFEENPSNASVSPVTIYPTPIPR
KCFDEAVQIQPVFNELYARITQDMAQPDSYLHKTTEALALSDSEFTGKLW
SLYLATLKSAQYKKQNFRLGIFRSDYLIDKKKGTEQIKQVEFNTVSVSFA
GLSEKVDRLHSYLNRANKYDPKGPIYNDQNMVISDSGYLLSKALAKAVES
YKSQQSDPIVAFIVQRNERNVFDQKVLELNLLEKFGTKSVRLTFDDVNDK
LFIDDKTGKLFIRDTEQEIAVVYYRTGYTTTDYTSEKDWEARLFLEKSFA
IKAPDLLTQLSGSKKIQQLLTDEGVLGKYISDAEKKSSLLKTFVKIYPLD
DTKLGREGKRLALSEPSKYVLKPQREGGGNNVYKENIPNFLKGIEERHWD
AYILMELIEPELNENNIILRDNKSYNEPIISELGIYGCVLFNDEQVLSNE
FSGSLLRSKFNTSNEGGVAAGFGCLDSIILY
3D structure
PDB1m0w Large Conformational Changes in the Catalytic Cycle of Glutathione Synthase
ChainA
Resolution1.8 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.3.2.3: glutathione synthase.
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 MG A E146 E386 E141 E376
BS02 ANP A L132 E146 K324 K382 E386 G387 N391 Y393 M415 L417 I418 E442 K469 L127 E141 K314 K372 E376 G377 N381 Y383 M405 L407 I408 E432 K459
BS03 3GC A R128 N148 S151 V152 S153 E228 Q234 R285 Y288 R123 N143 S146 V147 S148 E218 Q224 R275 Y278
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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