Structure of PDB 2dqn Chain A

Receptor sequence
>2dqnA (length=485) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
MSIRYESVENLLTLIKDKKIKPSDVVKDIYDAIEETDPTIKSFLALDKEN
AIKKAQELDELQAKDQMDGKLFGIPMGIKDNIITNGLETTCASKMLEGFV
PIYESTVMEKLHKENAVLIGKLNMDEFAMGGSTETSYFKKTVNPFDHKAV
PGGSSGGSAAAVAAGLVPLSLGSDTGGSIRQPAAYCGVVGMKPTYGRVSR
FGLVAFASSLDQIGPLTRNVKDNAIVLEAISGADVNDSTSAPVDDVDFTS
EIGKDIKGLKVALPKEYLGEGVADDVKEAVQNAVETLKSLGAVVEEVSLP
NTKFGIPSYYVIASSEASSNLSRFDGIRYGYHSKEAHSLEELYKMSRSEG
FGKEVKRRIFLGTFALSSGYYDAYYKKSQKVRTLIKNDFDKVFENYDVVV
GPTAPTTAFNLGEEIDDPLTMYANDLLTTPVNLAGLPGISVPCGQSNGRP
IGLQFIGKPFDEKTLYRVAYQYETQYNLHDVYEKL
3D structure
PDB2dqn Ammonia channel couples glutaminase with transamidase reactions in GatCAB
ChainA
Resolution2.55 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) K79 S154 S155 S173 T175 G176 G177 S178 Q181
Catalytic site (residue number reindexed from 1) K79 S154 S155 S173 T175 G176 G177 S178 Q181
Enzyme Commision number 6.3.5.7: glutaminyl-tRNA synthase (glutamine-hydrolyzing).
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 ASN A M129 G130 T175 G176 S178 Y309 Y310 R358 D425 M129 G130 T175 G176 S178 Y309 Y310 R358 D425
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0050567 glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
Biological Process
GO:0006412 translation
Cellular Component
GO:0030956 glutamyl-tRNA(Gln) amidotransferase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:2dqn, PDBe:2dqn, PDBj:2dqn
PDBsum2dqn
PubMed16809541
UniProtP63488|GATA_STAAM Glutamyl-tRNA(Gln) amidotransferase subunit A (Gene Name=gatA)

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