Structure of PDB 2wyo Chain A

Receptor sequence
>2wyoA (length=520) Species: 5691 (Trypanosoma brucei) [Search protein sequence]
NLYFQGHMVLKLLLELGAERYAEQFAAKCHELGMVMKESAGPGRVPVPVT
LQPSMISRGEFGTLCCMQPLWNEAVDNTARNFTFLRDALQETAASDVNFT
GKLLNMLQEVYLSGGPFQQLMLGIFRTDYMREGVYDKSTTASRWKNVEIN
TISCSFAGLSPLITEFHQHIAAYLQVLQKARGGVENMSWIWGKGNCRLER
SVSGDVVPKAIADAVRAWVEQQKFASLRASWEQVLDTAPVVLVVVQENER
NTADQYALLMRVLEEHRIRFIFRTLQELHLSLKLHSISPEQPPLAVVDGH
YPIAVAYFRSTYVPEDFPTDATWAARLSLERSSAIKCPSIPYHLLTFKKL
QQLLCDVDRVLVPVAFCGDSDKAGLLQRHFVPQYSLNPKEVGEEAVEKVI
HDVLQRPDQFVLKPQLEGGGNLLSGETMVTYSKVRCEYVVMSRIQFHVST
GSLLARGDVVQLERNMCSEVGIFGVILSAAKGSSVGTNGSSVLFNTFAGY
TVRSKPADAVAALDSLAVVP
3D structure
PDB2wyo Structure of Trypanosoma Brucei Glutathione Synthetase; Domain and Loop Alterations in the Catalytic Cycle of a Highly Conserved Enzyme.
ChainA
Resolution3.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) R119 E143 N145 S150 K363 K428 E432 G433 R530
Catalytic site (residue number reindexed from 1) R126 E148 N150 S155 K348 K413 E417 G418 R503
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 GSH A R119 S148 S150 E264 N266 R324 Y327 R530 R126 S153 S155 E249 N251 R309 Y312 R503
Gene Ontology
Molecular Function
GO:0000287 magnesium ion binding
GO:0004363 glutathione synthase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0043295 glutathione binding
GO:0046872 metal ion binding
Biological Process
GO:0006750 glutathione biosynthetic process
Cellular Component
GO:0005730 nucleolus
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:2wyo, PDBe:2wyo, PDBj:2wyo
PDBsum2wyo
PubMed20045436
UniProtQ57UN0

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