Structure of PDB 2g5i Chain B Binding Site BS02

Receptor Information
>2g5i Chain B (length=410) Species: 1280 (Staphylococcus aureus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HFETVIGLEVHVELKTDSKMFSPSPAHFGAEPNSNTNVIDLAYPGVLPVV
NKRAVDWAMRAAMALNMEIATESKFDRKNYFYPDNPKAYQISQFDQPIGE
NGYIDIEVDGETKRIGITRLHMEEDAGKSTHKGEYSLVDLNRQGTPLIEI
VSEPDIRSPKEAYAYLEKLRSIIQYTGVSDVKMEEGSLRCDANISLRPYG
QEKFGTKAELKNLNSFNYVRKGLEYEEKRQEEELLNGGEIGQETRRFDES
TGKTILMRVKEGSDDYRYFPEPDIVPLYIDDAWKERVRQTIPELPDERKA
KYVNELGLPAYDAHVLTLTKEMSDFFESTIEHGADVKLTSNWLMGGVNEY
LNKNQVELLDTKLTPENLAGMIKLIEDGTMSSKIAKKVFPELAAKGGNAK
QIMEDNGLVQ
Ligand information
Ligand IDADP
InChIInChI=1S/C10H15N5O10P2/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(24-10)1-23-27(21,22)25-26(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKeyXTWYTFMLZFPYCI-KQYNXXCUSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)[C@H]3[C@@H]([C@@H]([C@H](O3)CO[P@](=O)(O)OP(=O)(O)O)O)O)N
CACTVS 3.341Nc1ncnc2n(cnc12)[CH]3O[CH](CO[P](O)(=O)O[P](O)(O)=O)[CH](O)[CH]3O
ACDLabs 10.04O=P(O)(O)OP(=O)(O)OCC3OC(n2cnc1c(ncnc12)N)C(O)C3O
CACTVS 3.341Nc1ncnc2n(cnc12)[C@@H]3O[C@H](CO[P@@](O)(=O)O[P](O)(O)=O)[C@@H](O)[C@H]3O
OpenEye OEToolkits 1.5.0c1nc(c2c(n1)n(cn2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)O)O)O)N
FormulaC10 H15 N5 O10 P2
NameADENOSINE-5'-DIPHOSPHATE
ChEMBLCHEMBL14830
DrugBankDB16833
ZINCZINC000012360703
PDB chain2g5i Chain B Residue 601 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB2g5i Ammonia channel couples glutaminase with transamidase reactions in GatCAB
Resolution3.35 Å
Binding residue
(original residue number in PDB)		V6 E10 V152 S153 P155 N194 S196 K208
Binding residue
(residue number reindexed from 1)		V5 E9 V151 S152 P154 N193 S195 K207
Annotation score5
Enzymatic activity
Enzyme Commision number 6.3.5.-
Gene Ontology
Molecular Function
GO:0003824 catalytic activity
GO:0005524 ATP binding
GO:0016874 ligase activity
GO:0016884 carbon-nitrogen ligase activity, with glutamine as amido-N-donor
GO:0050566 asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity
GO:0050567 glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity
Biological Process
GO:0006412 translation
GO:0070681 glutaminyl-tRNAGln biosynthesis via transamidation

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Molecular Function
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Biological Process
External links
PDB RCSB:2g5i, PDBe:2g5i, PDBj:2g5i
PDBsum2g5i
PubMed16809541
UniProtP64201|GATB_STAAM Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B (Gene Name=gatB)

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