5JY0

Crystal structure of Porphyromonas endodontalis DPP11 in complex with substrate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004177	molecular_function	aminopeptidase activity
A	0005576	cellular_component	extracellular region
A	0006508	biological_process	proteolysis
A	0008236	molecular_function	serine-type peptidase activity
A	0008239	molecular_function	dipeptidyl-peptidase activity
A	0009986	cellular_component	cell surface
A	0043171	biological_process	peptide catabolic process
A	0070009	molecular_function	serine-type aminopeptidase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue TRS A 801

Chain	Residue
A	THR277
A	ARG336
A	THR648
A	GLY649
A	ASP678

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site_id	AC2
Number of Residues	7
Details	binding site for residue TRS A 802

Chain	Residue
A	ASN632
A	SER633
A	ARG694
A	GLN261
A	GLY262
A	VAL263
A	LYS595

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Charge relay system => ECO:0000250|UniProtKB:V5YM14

Chain	Residue	Details
A	HIS85
A	ASP226

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Charge relay system => ECO:0000250|UniProtKB:V5YM14, ECO:0000305|PubMed:21896480

Chain	Residue	Details
A	ALA652

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site_id	SWS_FT_FI3
Number of Residues	1
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:0000250|UniProtKB:B2RID1, ECO:0000305|PubMed:21896480

Chain	Residue	Details
A	ARG670

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