Structure of PDB 2f2a Chain A Binding Site BS01

Receptor Information
>2f2a 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 IDGLN
InChIInChI=1S/C5H10N2O3/c6-3(5(9)10)1-2-4(7)8/h3H,1-2,6H2,(H2,7,8)(H,9,10)/t3-/m0/s1
InChIKeyZDXPYRJPNDTMRX-VKHMYHEASA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(CC(=O)N)C(C(=O)O)N
OpenEye OEToolkits 1.5.0C(CC(=O)N)[C@@H](C(=O)O)N
ACDLabs 10.04O=C(N)CCC(N)C(=O)O
CACTVS 3.341N[CH](CCC(N)=O)C(O)=O
CACTVS 3.341N[C@@H](CCC(N)=O)C(O)=O
FormulaC5 H10 N2 O3
NameGLUTAMINE
ChEMBLCHEMBL930
DrugBankDB00130
ZINCZINC000001532526
PDB chain2f2a Chain A Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2f2a Ammonia channel couples glutaminase with transamidase reactions in GatCAB
Resolution2.3 Å
Binding residue
(original residue number in PDB)		G130 S154 D174 T175 G176 S178 F206 Y309 Y310 R358 D425
Binding residue
(residue number reindexed from 1)		G130 S154 D174 T175 G176 S178 F206 Y309 Y310 R358 D425
Annotation score5
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

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:2f2a, PDBe:2f2a, PDBj:2f2a
PDBsum2f2a
PubMed16809541
UniProtP63488|GATA_STAAM Glutamyl-tRNA(Gln) amidotransferase subunit A (Gene Name=gatA)

[Back to BioLiP]