Structure of PDB 5dm3 Chain E

Receptor sequence
>5dm3E (length=383) Species: 290398 (Chromohalobacter israelensis DSM 3043) [Search protein sequence]
TLALDDLKTRVESGEIDTVLVCIVDMQGRLMGKRLHARHFVDHGWEETHC
YLLYIMKPDLATLRCVPWLEGTAMVLCDLLDHAEVPHAPRAILKRQLARL
EAMGLEAIMATELEFFLFEKSLDETTKEEHVLRPLRNHLHAAGIPVEGTK
GEAGAGQEELNIRCAKALDTADYHTIAKHATKEIAWQQGRAVTFLSKWHH
AHAGSSSHIHQSLWKQGLPAFHLGMSALMKHYLAGLLKYAPDYTYFLAPY
LNSYKRFQTFAPTRTVWSVDNRTAGFRLCAEGTRAVRIECRIGGSDLNPY
LAMAGQLAAGIKGIEECLALPPPAEGDLIPQNLRDAMEALRGSTMLREAM
GEDVVDHYVRAAEVELEDFQRVVSDYEVARGFE
3D structure
PDB5dm3 Crystal Structure of Glutamine Synthetase from Chromohalobacter salexigens DSM 3043(Csal_0679, TARGET EFI-550015) with bound ADP
ChainE
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) E143 E145 E206 E213 H262 R333 E350 R352
Catalytic site (residue number reindexed from 1) E112 E114 E152 E159 H208 R272 E289 R291
Enzyme Commision number 6.3.1.2: glutamine synthetase.
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 ADP E E143 E201 R217 C218 H264 R348 E112 E147 R163 C164 H210 R287
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0003824 catalytic activity
GO:0004356 glutamine synthetase activity
GO:0016874 ligase activity
GO:0016879 ligase activity, forming carbon-nitrogen bonds
Biological Process
GO:0006542 glutamine biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:5dm3, PDBe:5dm3, PDBj:5dm3
PDBsum5dm3
PubMed
UniProtQ1QZR8

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