4XZY

Crystal structure of dipeptidyl peptidase 11 (DPP11) from Porphyromonas gingivalis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008239	molecular_function	dipeptidyl-peptidase activity
A	0070009	molecular_function	serine-type aminopeptidase activity
B	0008239	molecular_function	dipeptidyl-peptidase activity
B	0070009	molecular_function	serine-type aminopeptidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	binding site for residue GOL A 801

Chain	Residue
A	TRP395
A	ASP546

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"UniProtKB","id":"V5YM14","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"26057589","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"UniProtKB","id":"V5YM14","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"21896480","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"26057589","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Site: {"description":"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","evidences":[{"source":"PubMed","id":"26057589","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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