Structure of PDB 5dm3 Chain D

Receptor sequence
>5dm3D (length=386) Species: 290398 (Chromohalobacter israelensis DSM 3043) [Search protein sequence]
TLALDDLKTRVESGEIDTVLVCIVDMQGRLMGKRLHARHFVDHGWEETHC
CNYLYIMKPDLATLRCVPWLEGTAMVLCDLLDHRTHAEVPHAPRAILKRQ
LARLEAMGLEAIMATELEFFLFEKSLDTTKEEHVLRPLRNHLHAAGIPVE
GTKGEAGAGQEELNIRCAKALDTADYHTIAKHATKEIAWQQGRAVTFLSK
WHHAHAGSSSHIHQSLWKQGLPAFHDERDALGMSALMKHYLAGLLKYAPD
YTYFLAPYLNSYKRFAPTRTVWSVDNRTAGFRLCAEGTRAVRIECRIGGS
DLNPYLAMAGQLAAGIKGIEECLALPPPAELIPQNLRDAMEALRGSTMLR
EAMGEDVVDHYVRAAEVELEDFQRVVSDYEVARGFE
3D structure
PDB5dm3 Crystal Structure of Glutamine Synthetase from Chromohalobacter salexigens DSM 3043(Csal_0679, TARGET EFI-550015) with bound ADP
ChainD
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) E116 E118 E155 E162 H211 R277 E294 R296
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 D T51 H52 T48 H49
BS02 ADP D I139 A141 E143 R217 C218 S266 R348 I112 A114 E116 R166 C167 S215 R292
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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