5HXD

Crystal structure of murein-tripeptide amidase MpaA from Escherichia coli O157

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004040	molecular_function	amidase activity
A	0004180	molecular_function	carboxypeptidase activity
A	0004181	molecular_function	metallocarboxypeptidase activity
A	0005737	cellular_component	cytoplasm
A	0006508	biological_process	proteolysis
A	0008237	molecular_function	metallopeptidase activity
A	0008270	molecular_function	zinc ion binding
A	0009253	biological_process	peptidoglycan catabolic process
A	0016998	biological_process	cell wall macromolecule catabolic process
A	0046872	molecular_function	metal ion binding
A	0061473	molecular_function	murein tripeptide carboxypeptidase activity
A	0071555	biological_process	cell wall organization
B	0004040	molecular_function	amidase activity
B	0004180	molecular_function	carboxypeptidase activity
B	0004181	molecular_function	metallocarboxypeptidase activity
B	0005737	cellular_component	cytoplasm
B	0006508	biological_process	proteolysis
B	0008237	molecular_function	metallopeptidase activity
B	0008270	molecular_function	zinc ion binding
B	0009253	biological_process	peptidoglycan catabolic process
B	0016998	biological_process	cell wall macromolecule catabolic process
B	0046872	molecular_function	metal ion binding
B	0061473	molecular_function	murein tripeptide carboxypeptidase activity
B	0071555	biological_process	cell wall organization

Functional Information from PDB Data

site_id	AC2
Number of Residues	8
Details	binding site for residue CAC A 302

site_id	AC4
Number of Residues	5
Details	binding site for residue CAC B 302

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton donor/acceptor => ECO:0000255\|PROSITE-ProRule:PRU01379

site_id	SWS_FT_FI2
Number of Residues	6
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU01379