Structure of PDB 6gs2 Chain D Binding Site BS01

Receptor Information
>6gs2 Chain D (length=384) Species: 158879 (Staphylococcus aureus subsp. aureus N315) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DVLRKLAEQVDDIVFISGTNGKTTTSNLIGHTLKANNIQIIHNNEGANMA
AGITSAFIMQSTPKTKIAVIEIDEGSIPRVLKEVTPSMMVFTNFFRFGEI
DIMVNNIAETISNKGIKLLLNADDPFVSRLKIASDTIVYYGMKAHAHEFE
RYCPNCGRLLQYDYIHYNQIGHYHCQCGFKREQAKYEISSFDVAPFLYLN
INDEKYDMKIAGDFNAYNALAAYTVLRELGLNEQTIKNGFETYTSDNGRM
QYFKKERKEAMINLAKNPAGMNASLSVGEQLEGEKVYVISLNDNAADGRD
TSWIYDADFEKLSKQQIEAIIVTGTRAEELQLRLKLAEVEVPIIVERDIY
KATAKTMDYKGFTVAIPNYTSLAPMLEQLNRSFE
Ligand information
Ligand IDZN
InChIInChI=1S/Zn/q+2
InChIKeyPTFCDOFLOPIGGS-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Zn++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Zn+2]
FormulaZn
NameZINC ION
ChEMBLCHEMBL1236970
DrugBankDB14532
ZINC
PDB chain6gs2 Chain D Residue 501 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB6gs2 Structural basis of cell wall peptidoglycan amidation by the GatD/MurT complex of Staphylococcus aureus.
Resolution2.04 Å
Binding residue
(original residue number in PDB)		C202 C205 C224 C226
Binding residue
(residue number reindexed from 1)		C153 C156 C175 C177
Annotation score1
Enzymatic activity
Enzyme Commision number 6.3.5.13: lipid II isoglutaminyl synthase (glutamine-hydrolyzing).
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:6gs2, PDBe:6gs2, PDBj:6gs2
PDBsum6gs2
PubMed30154570
UniProtA0A0H3JUU7|MURT_STAAN Lipid II isoglutaminyl synthase (glutamine-hydrolyzing) subunit MurT (Gene Name=murT)

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