Structure of PDB 6h5e Chain D

Receptor sequence
>6h5eD (length=394) Species: 1280 (Staphylococcus aureus) [Search protein sequence]
DTDVLRKLAEQVDDIVFISGTNGKTTTSNLIGHTLKANNIQIIHNNEGAN
MAAGITSAFIMQSTPKTKIAVIEIDEGSIPRVLKEVTPSMMVFTNFFRDQ
MDRFGEIDIMVNNIAETISNKGIKLLLNADDPFVSRLKIASDTIVYYGMK
AHAHEFEESRYCPNCGRLLQYDYIHYNQIGHYHCQCGFKREQAKYEISSF
DVAPFLYLNINDEKYDMKIAGDFNAYNALAAYTVLRELGLNEQTIKNGFE
TYTSDNGRMQYFKKERKEAMINLAKNPAGMNASLSVGEQLEGEKVYVISL
NDNAADGRDTSWIYDADFEKLSKQQIEAIIVTGTRAEELQLRLKLAEVEV
PIIVERDIYKATAKTMDYKGFTVAIPNYTSLAPMLEQLNRSFEG
3D structure
PDB6h5e Structural basis of cell wall peptidoglycan amidation by the GatD/MurT complex of Staphylococcus aureus.
ChainD
Resolution2.139 Å
3D
structure
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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 D C202 C205 C224 C226 C162 C165 C184 C186
BS02 ANP D N57 G58 K59 T60 E108 N130 F132 Y216 F263 N267 N22 G23 K24 T25 E73 N95 F97 Y176 F223 N227
BS03 MG D T60 E108 T25 E73
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:6h5e, PDBe:6h5e, PDBj:6h5e
PDBsum6h5e
PubMed30154570
UniProtA0A0H3JUU7|MURT_STAAN Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT (Gene Name=murT)

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