Structure of PDB 7q8e Chain C

Receptor sequence
>7q8eC (length=397) Species: 93062 (Staphylococcus aureus subsp. aureus COL) [Search protein sequence]
DILRKLAEQVDDIVFISGTNGKTTTSNLIGHTLKANNIQIIHNNEGANMA
AGITSAFIMQSTPKTKIAVIEIDEGSIPRVLKEVTPSMMVFTNFFRDQMD
RFGEIDIMVNNIAETISNKGIKLLLNADDPFVSRLKIASDTIVYYGMKAH
AHEFEQSTMNESRYCPNCGRLLQYDYIHYNQIGHYHCQCGFKREQAKYEI
SSFDVAPFLYLNINDEKYDMKIAGDFNAYNALAAYTVLRELGLNEQTIKN
GFETYTSDNGRMQYFKKERKEAMINLAKNPAGMNASLSVGEQLEGEKVYV
ISLNDNAADGRDTSWIYDADFEKLSKQQIEAIIVTGTRAEELQLRLKLAE
VEVPIIVERDIYKATAKTMDYKGFTVAIPNYTSLAPMLEQLNRSFEG
3D structure
PDB7q8e Crystal Structure of the MurT-GatD Enzyme Complex from Staphylococcus aureus COL strain
ChainC
Resolution2.90002 Å
3D
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Enzymatic activity
Enzyme Commision number 6.3.5.13: lipid II isoglutaminyl 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 ZN C C202 C224 C226 C165 C187 C189
Gene Ontology
Molecular Function
GO:0005524 ATP binding
GO:0008270 zinc ion binding
GO:0016874 ligase activity
GO:0016879 ligase activity, forming carbon-nitrogen bonds
GO:0016881 acid-amino acid ligase activity
GO:0046872 metal ion binding
GO:0140282 carbon-nitrogen ligase activity on lipid II
Biological Process
GO:0008360 regulation of cell shape
GO:0009058 biosynthetic process
GO:0009252 peptidoglycan biosynthetic process
GO:0071555 cell wall organization

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Molecular Function
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Biological Process
External links
PDB RCSB:7q8e, PDBe:7q8e, PDBj:7q8e
PDBsum7q8e
PubMed
UniProtA0A0H2WZQ7|MURT_STAAC Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT (Gene Name=murT)

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