Structure of PDB 3nzt Chain A

Receptor sequence
>3nztA (length=498) Species: 119856 (Francisella tularensis subsp. tularensis) [Search protein sequence]
YDFKKINNLRGIERETLRVTDCGNLATSNHPDGLGHKLTNNSITVDFSEN
LLELITKPHDSIDKAIGELYQLSAFTLDNMHSDEIILNTSMPLSANDNDI
QEADFGSSNSGRMKRVYRKGLSARYGKIMQIISGIHYNFSFDKDLISNIA
TNKQVSISDIYFDVLNNYFEFMWLLPYLFGASPICAKTSVKNKPDYLSVL
DDKFYVGEYATSLRMSDLGSPAQKDLAISYDNVKAYVKDLIQATDDTFAD
YKRIGLYNSQGQRIQLNDGILQIENEYYSAIRPKQIAKRGERPACALYNR
GVEYVEVRVLDVDPFEPVGISKDTALFVEVMLMTCLDKDAKKYHKDIIKQ
AKQNLTAVAIQGRNPQLKLKKLDDDSEILLKDYALELFDEIEAVAKKMPK
EYLDAVEIQKRKVLDISQTPSAKIIELARQHGYKKFILDISRRVSQQFRS
YELPAAIVAKLKDQAGQSVAAEKELVANDKISLDEYINRYYKSSKGCC
3D structure
PDB3nzt 2.0 Angstrom Crystal structure of Glutamate--Cysteine Ligase (gshA) ftom Francisella tularensis in Complex with AMP.
ChainA
Resolution2.0 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 AMP A I56 T57 K58 P59 N139 F140 S141 I289 Y307 I55 T56 K57 P58 N138 F139 S140 I286 Y304
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0004357 glutamate-cysteine ligase activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0016879 ligase activity, forming carbon-nitrogen bonds
GO:0046872 metal ion binding
Biological Process
GO:0006750 glutathione biosynthetic process
Cellular Component
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:3nzt, PDBe:3nzt, PDBj:3nzt
PDBsum3nzt
PubMed
UniProtQ5NHS8

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