Structure of PDB 2dqn Chain A Binding Site BS01

Receptor Information
>2dqn Chain A (length=485) Species: 1280 (Staphylococcus aureus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MSIRYESVENLLTLIKDKKIKPSDVVKDIYDAIEETDPTIKSFLALDKEN
AIKKAQELDELQAKDQMDGKLFGIPMGIKDNIITNGLETTCASKMLEGFV
PIYESTVMEKLHKENAVLIGKLNMDEFAMGGSTETSYFKKTVNPFDHKAV
PGGSSGGSAAAVAAGLVPLSLGSDTGGSIRQPAAYCGVVGMKPTYGRVSR
FGLVAFASSLDQIGPLTRNVKDNAIVLEAISGADVNDSTSAPVDDVDFTS
EIGKDIKGLKVALPKEYLGEGVADDVKEAVQNAVETLKSLGAVVEEVSLP
NTKFGIPSYYVIASSEASSNLSRFDGIRYGYHSKEAHSLEELYKMSRSEG
FGKEVKRRIFLGTFALSSGYYDAYYKKSQKVRTLIKNDFDKVFENYDVVV
GPTAPTTAFNLGEEIDDPLTMYANDLLTTPVNLAGLPGISVPCGQSNGRP
IGLQFIGKPFDEKTLYRVAYQYETQYNLHDVYEKL
Ligand information
Ligand IDASN
InChIInChI=1S/C4H8N2O3/c5-2(4(8)9)1-3(6)7/h2H,1,5H2,(H2,6,7)(H,8,9)/t2-/m0/s1
InChIKeyDCXYFEDJOCDNAF-REOHCLBHSA-N
SMILES
SoftwareSMILES
CACTVS 3.370N[C@@H](CC(N)=O)C(O)=O
ACDLabs 12.01O=C(N)CC(N)C(=O)O
CACTVS 3.370N[CH](CC(N)=O)C(O)=O
OpenEye OEToolkits 1.7.2C(C(C(=O)O)N)C(=O)N
OpenEye OEToolkits 1.7.2C([C@@H](C(=O)O)N)C(=O)N
FormulaC4 H8 N2 O3
NameASPARAGINE
ChEMBLCHEMBL58832
DrugBankDB00174
ZINCZINC000001532556
PDB chain2dqn Chain A Residue 511 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB2dqn Ammonia channel couples glutaminase with transamidase reactions in GatCAB
Resolution2.55 Å
Binding residue
(original residue number in PDB)		M129 G130 T175 G176 S178 Y309 Y310 R358 D425
Binding residue
(residue number reindexed from 1)		M129 G130 T175 G176 S178 Y309 Y310 R358 D425
Annotation score3
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).
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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