5SDK

PanDDA analysis group deposition -- Crystal Structure of Porphyromonas gingivalis in complex with Z416341642

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004177	molecular_function	aminopeptidase activity
A	0006508	biological_process	proteolysis
A	0008233	molecular_function	peptidase activity
A	0008236	molecular_function	serine-type peptidase activity
A	0008239	molecular_function	dipeptidyl-peptidase activity
A	0009986	cellular_component	cell surface
A	0016787	molecular_function	hydrolase activity
A	0042277	molecular_function	peptide binding
A	0043171	biological_process	peptide catabolic process
A	0048588	biological_process	developmental cell growth
A	0070009	molecular_function	serine-type aminopeptidase activity
B	0004177	molecular_function	aminopeptidase activity
B	0006508	biological_process	proteolysis
B	0008233	molecular_function	peptidase activity
B	0008236	molecular_function	serine-type peptidase activity
B	0008239	molecular_function	dipeptidyl-peptidase activity
B	0009986	cellular_component	cell surface
B	0016787	molecular_function	hydrolase activity
B	0042277	molecular_function	peptide binding
B	0043171	biological_process	peptide catabolic process
B	0048588	biological_process	developmental cell growth
B	0070009	molecular_function	serine-type aminopeptidase activity

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Charge relay system => ECO:0000250\|UniProtKB:V5YM14, ECO:0000305\|PubMed:26057589

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Charge relay system => ECO:0000250\|UniProtKB:V5YM14, ECO:0000305\|PubMed:21896480, ECO:0000305\|PubMed:26057589

site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Is essential for the Asp/Glu P1 specificity of DPP11; involved in the recognition of the Asp/Glu residue at the P1 position of substrate peptides => ECO:0000269\|PubMed:26057589