Structure of PDB 3ig5 Chain A

Receptor sequence
>3ig5A (length=672) Species: 4932 (Saccharomyces cerevisiae) [Search protein sequence]
GLLALGTPLQWFESRTYNEHIRDEGIEQLLYIFQAAGKRDNDPLFWGDEL
EYMVVDFDDKERNSMLDVCHDKILTELNMEDSSLCEANDVSFHPEYGRYM
LEATPASPYLNYVGSYVEVNMQKRRAIAEYKLSEYARQDSKNNLHVGSRS
VPLTLTVFPRMGCPDFINIKDPWNHKNAASRSLFLPDEVINRHVRFPNLT
ASIRTRRGEKVCMNVPMYKDIATPETDDSIYDRDWFLPEDKEAKLASKPG
FIYMDSMGFGMGCSCLQVTFQAPNINKARYLYDALVNFAPIMLAFSAAAP
AFKGWLADQDVRWNVISGAVDDRTPKERGVAPLLPKYNKNGFGGIAKDVQ
DKVLEIPKSRYSSVDLFLGGSKFFNRTYNDTNVPINEKVLGRLLENDKAP
LDYDLAKHFAHLYIRDPVSTFEELLNQDNKTSSNHFENIQSTNWQTLRFK
PPTQQATPDKKDSPGWRVEFRPFEVQLLDFENAAYSVLIYLIVDSILTFS
DNINAYIHMSKVWENMKIAHHRDAILFEKFHWKKSFRNDTDVETEDYSIS
EIFHNPENGIFPQFVTPILCQKGFVTKDWKELKHSSKHERLYYYLKLISD
RASGELPTTAKFFRNFVLQHPDYKHDSKISKSINYDLLSTCDRLTHLDDS
KGELTSFLGAEIAEYVKKNKPS
3D structure
PDB3ig5 Mechanistic details of glutathione biosynthesis revealed by crystal structures of Saccharomyces cerevisiae glutamate cysteine ligase.
ChainA
Resolution2.1 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 6.3.2.2: glutamate--cysteine ligase.
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 GLU A E52 C266 Q268 R313 I317 E51 C265 Q267 R312 I316
BS02 MG A E52 E96 E103 E51 E95 E102
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004357 glutamate-cysteine ligase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
Biological Process
GO:0006750 glutathione biosynthetic process
GO:0042542 response to hydrogen peroxide
GO:0046686 response to cadmium ion
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3ig5, PDBe:3ig5, PDBj:3ig5
PDBsum3ig5
PubMed19726687
UniProtP32477|GSH1_YEAST Glutamate--cysteine ligase (Gene Name=GSH1)

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