Structure of PDB 2g5h Chain B Binding Site BS01

Receptor Information

>2g5h Chain B (length=398) Species: 1280 (Staphylococcus aureus)

FETVIGLEVHVELKTDSKMFSPSPAHFGAEPNSNTNVIDLAYPGVLPVVN
KRAVDWAMRAAMALNMEIATESKFDRKNYFYPDNPKAYQISQFDQPIGEN
GYIDIEVDGETKRIGITRLHMEEDAGKSTHKGEYSLVDLNRQGTPLIEIV
SEPDIRSPKEAYAYLEKLRSIIQYTGVSDVKMEEGSLRCDANISLRPYGQ
EKFGTKAELKNLNSFNYVRKGLEYEEKRQEEELLNGGEIGQETRRFDEST
GKTILMRVKEGSDDYRYFPEPDIVPLYIDDAWKERVRQTIPELPDERKAK
YVNELGLPAYDAHVLTLTKEMSDFFESTIEHGADVKLTSNWLMGGVNEYL
NKNQVELLDTKLTPENLAGMIKLIEDGTMSSKIAKKVFPELAAKGGNA

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 2g5h Chain B Residue 501

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2g5h Ammonia channel couples glutaminase with transamidase reactions in GatCAB
• Resolution: 2.5 Å
• Binding residue (original residue number in PDB): H12 E124 E150
• Binding residue (residue number reindexed from 1): H10 E122 E148
• Annotation score: 1

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

External links

• PDB: RCSB:2g5h, PDBe:2g5h, PDBj:2g5h
• PDBsum: 2g5h
• PubMed: 16809541
• UniProt: P64201|GATB_STAAM Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B (Gene Name=gatB)