1E0D

UDP-N-Acetylmuramoyl-L-Alanine:D-Glutamate Ligase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0008360	biological_process	regulation of cell shape
A	0008764	molecular_function	UDP-N-acetylmuramoylalanine-D-glutamate ligase activity
A	0009058	biological_process	biosynthetic process
A	0009252	biological_process	peptidoglycan biosynthetic process
A	0016874	molecular_function	ligase activity
A	0016881	molecular_function	acid-amino acid ligase activity
A	0042802	molecular_function	identical protein binding
A	0051301	biological_process	cell division
A	0071555	biological_process	cell wall organization

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A 800

Chain	Residue
A	LYS115
A	SER159
A	SER160
A	TYR194
A	LYS198

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Functional Information from PROSITE/UniProt

site_id	PS00012
Number of Residues	16
Details	PHOSPHOPANTETHEINE Phosphopantetheine attachment site. GSNGKSTVTTLVGEMA

Chain	Residue	Details
A	GLY111-ALA126

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	1
Details	Annotated By Reference To The Literature 1p3d

Chain	Residue	Details
A	LYS115

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site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1p3d

Chain	Residue	Details
A	ASN138
A	LYS115

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site_id	MCSA1
Number of Residues	2
Details	M-CSA 317

Chain	Residue	Details
A	LYS115	activator, attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase electrophilicity
A	ASN138	electrostatic stabiliser, hydrogen bond donor, steric role

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