Structure of PDB 5dm3 Chain B

Receptor sequence
>5dm3B (length=385) Species: 290398 (Chromohalobacter israelensis DSM 3043) [Search protein sequence]
NTLALDDLKTRVESGEIDTVLVCIVDMQGRLMGKRLHARHFVDHGWEETH
CCYIMKPDLATLRCVPWLEGTAMVLCDLLDHAEVPHAPRAILKRQLARLE
AMGLEAIMATELEFFLFEKSLDETTKEEHVLRPLRNHLHAAGIPVEGTKG
EAGQEELNIRCAKALDTADYHTIAKHATKEIAWQQGRAVTFLSKWHHAHA
GSSSHIHQSLWKQGLPAFHDERDALGMSALMKHYLAGLLKYAPDYTYFLA
PYLNSYKRFQKGTFAPTRTVWSVDNRTAGFRLCAEGTRAVRIECRIGGSD
LNPYLAMAGQLAAGIKGIEECLALPPPAGLIPQNLRDAMEALRGSTMLRE
AMGEDVVDHYVRAAEVELEDFQRVVSDYEVARGFE
3D structure
PDB5dm3 Crystal Structure of Glutamine Synthetase from Chromohalobacter salexigens DSM 3043(Csal_0679, TARGET EFI-550015) with bound ADP
ChainB
Resolution2.6 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) E143 E145 E206 E213 H262 R333 E350 R352
Catalytic site (residue number reindexed from 1) E111 E113 E151 E156 H205 R276 E293 R295
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 B I139 A141 E201 R217 C218 H264 S266 R348 I107 A109 E146 R160 C161 H207 S209 R291
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

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

[Back to BioLiP]