Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6FQB

MurT/GatD peptidoglycan amidotransferase complex from Streptococcus pneumoniae R6

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0005524	molecular_function	ATP binding
A	0008270	molecular_function	zinc ion binding
A	0008360	biological_process	regulation of cell shape
A	0009058	biological_process	biosynthetic process
A	0009252	biological_process	peptidoglycan biosynthetic process
A	0016874	molecular_function	ligase activity
A	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
A	0016881	molecular_function	acid-amino acid ligase activity
A	0046872	molecular_function	metal ion binding
A	0071555	biological_process	cell wall organization
A	0140282	molecular_function	carbon-nitrogen ligase activity on lipid II
B	0000166	molecular_function	nucleotide binding
B	0005524	molecular_function	ATP binding
B	0008270	molecular_function	zinc ion binding
B	0008360	biological_process	regulation of cell shape
B	0009058	biological_process	biosynthetic process
B	0009252	biological_process	peptidoglycan biosynthetic process
B	0016874	molecular_function	ligase activity
B	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
B	0016881	molecular_function	acid-amino acid ligase activity
B	0046872	molecular_function	metal ion binding
B	0071555	biological_process	cell wall organization
B	0140282	molecular_function	carbon-nitrogen ligase activity on lipid II
C	0000166	molecular_function	nucleotide binding
C	0005524	molecular_function	ATP binding
C	0008270	molecular_function	zinc ion binding
C	0008360	biological_process	regulation of cell shape
C	0009058	biological_process	biosynthetic process
C	0009252	biological_process	peptidoglycan biosynthetic process
C	0016874	molecular_function	ligase activity
C	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
C	0016881	molecular_function	acid-amino acid ligase activity
C	0046872	molecular_function	metal ion binding
C	0071555	biological_process	cell wall organization
C	0140282	molecular_function	carbon-nitrogen ligase activity on lipid II
D	0000166	molecular_function	nucleotide binding
D	0005524	molecular_function	ATP binding
D	0008270	molecular_function	zinc ion binding
D	0008360	biological_process	regulation of cell shape
D	0009058	biological_process	biosynthetic process
D	0009252	biological_process	peptidoglycan biosynthetic process
D	0016874	molecular_function	ligase activity
D	0016879	molecular_function	ligase activity, forming carbon-nitrogen bonds
D	0016881	molecular_function	acid-amino acid ligase activity
D	0046872	molecular_function	metal ion binding
D	0071555	biological_process	cell wall organization
D	0140282	molecular_function	carbon-nitrogen ligase activity on lipid II
E	0003824	molecular_function	catalytic activity
E	0004359	molecular_function	glutaminase activity
E	0008360	biological_process	regulation of cell shape
E	0009236	biological_process	cobalamin biosynthetic process
E	0009252	biological_process	peptidoglycan biosynthetic process
E	0016787	molecular_function	hydrolase activity
E	0016874	molecular_function	ligase activity
E	0071555	biological_process	cell wall organization
E	0140282	molecular_function	carbon-nitrogen ligase activity on lipid II
F	0003824	molecular_function	catalytic activity
F	0004359	molecular_function	glutaminase activity
F	0008360	biological_process	regulation of cell shape
F	0009236	biological_process	cobalamin biosynthetic process
F	0009252	biological_process	peptidoglycan biosynthetic process
F	0016787	molecular_function	hydrolase activity
F	0016874	molecular_function	ligase activity
F	0071555	biological_process	cell wall organization
F	0140282	molecular_function	carbon-nitrogen ligase activity on lipid II
G	0003824	molecular_function	catalytic activity
G	0004359	molecular_function	glutaminase activity
G	0008360	biological_process	regulation of cell shape
G	0009236	biological_process	cobalamin biosynthetic process
G	0009252	biological_process	peptidoglycan biosynthetic process
G	0016787	molecular_function	hydrolase activity
G	0016874	molecular_function	ligase activity
G	0071555	biological_process	cell wall organization
G	0140282	molecular_function	carbon-nitrogen ligase activity on lipid II
H	0003824	molecular_function	catalytic activity
H	0004359	molecular_function	glutaminase activity
H	0008360	biological_process	regulation of cell shape
H	0009236	biological_process	cobalamin biosynthetic process
H	0009252	biological_process	peptidoglycan biosynthetic process
H	0016787	molecular_function	hydrolase activity
H	0016874	molecular_function	ligase activity
H	0071555	biological_process	cell wall organization
H	0140282	molecular_function	carbon-nitrogen ligase activity on lipid II

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	binding site for residue GLN E 301

Chain	Residue
E	CYS107
E	GLN111
E	ARG142
E	ASN163
E	GLN165
E	GLY166
E	HIS206

site_id	AC2
Number of Residues	8
Details	binding site for residue GLN F 301

Chain	Residue
F	ARG142
F	ASN163
F	HIS164
F	GLN165
F	GLY166
F	HIS206
F	CYS107
F	GLN111

site_id	AC3
Number of Residues	7
Details	binding site for residue GLN G 301

Chain	Residue
G	CYS107
G	GLN111
G	ARG142
G	ASN163
G	GLN165
G	GLY166
G	HIS206

site_id	AC4
Number of Residues	8
Details	binding site for residue GLN H 301

Chain	Residue
H	GLN79
H	CYS107
H	GLN111
H	ARG142
H	ASN163
H	GLN165
H	GLY166
H	HIS206

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"evidences":[{"source":"UniProtKB","id":"A0A0H3JUU7","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_02214","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"A0A0H3JUU7","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_02214","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_02213","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00606","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"30093673","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	4
Details	Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02213","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00606","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"30093673","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02213","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"30093673","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	792
Details	Domain: {"description":"GATase cobBQ-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00606","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)