4QR8

Crystal Structure of E coli pepQ

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004177	molecular_function	aminopeptidase activity
A	0005515	molecular_function	protein binding
A	0005829	cellular_component	cytosol
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0008235	molecular_function	metalloexopeptidase activity
A	0016795	molecular_function	phosphoric triester hydrolase activity
A	0016805	molecular_function	dipeptidase activity
A	0030145	molecular_function	manganese ion binding
A	0042803	molecular_function	protein homodimerization activity
A	0043171	biological_process	peptide catabolic process
A	0070573	molecular_function	metallodipeptidase activity
A	0102009	molecular_function	proline dipeptidase activity
B	0004177	molecular_function	aminopeptidase activity
B	0005515	molecular_function	protein binding
B	0005829	cellular_component	cytosol
B	0006508	biological_process	proteolysis
B	0008233	molecular_function	peptidase activity
B	0008235	molecular_function	metalloexopeptidase activity
B	0016795	molecular_function	phosphoric triester hydrolase activity
B	0016805	molecular_function	dipeptidase activity
B	0030145	molecular_function	manganese ion binding
B	0042803	molecular_function	protein homodimerization activity
B	0043171	biological_process	peptide catabolic process
B	0070573	molecular_function	metallodipeptidase activity
B	0102009	molecular_function	proline dipeptidase activity

Functional Information from PDB Data

Functional Information from PROSITE/UniProt

site_id	PS00491
Number of Residues	13
Details	PROLINE_PEPTIDASE Aminopeptidase P and proline dipeptidase signature. HGIGHpLGLqVHD

Chain	Residue	Details
A	HIS335-ASP347

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	10
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details