7Q8E

Crystal Structure of the MurT-GatD Enzyme Complex from Staphylococcus aureus COL strain

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	0003824	molecular_function	catalytic activity
B	0004359	molecular_function	glutaminase activity
B	0008360	biological_process	regulation of cell shape
B	0009236	biological_process	cobalamin biosynthetic process
B	0009252	biological_process	peptidoglycan biosynthetic process
B	0016787	molecular_function	hydrolase activity
B	0016874	molecular_function	ligase activity
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	0003824	molecular_function	catalytic activity
D	0004359	molecular_function	glutaminase activity
D	0008360	biological_process	regulation of cell shape
D	0009236	biological_process	cobalamin biosynthetic process
D	0009252	biological_process	peptidoglycan biosynthetic process
D	0016787	molecular_function	hydrolase activity
D	0016874	molecular_function	ligase activity
D	0071555	biological_process	cell wall organization
D	0140282	molecular_function	carbon-nitrogen ligase activity on lipid II

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"evidences":[{"source":"UniProtKB","id":"A0A0H3JUU7","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_02214","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	8
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_FI3
Number of Residues	382
Details	Domain: {"description":"GATase cobBQ-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00606","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
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":"29593310","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02213","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU00606","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"29593310","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_02213","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"29593310","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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