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6JTC

Crystal structure of dipeptidyl peptidase 11 (DPP11) with SH-5 from Porphyromonas gingivalis (Space)

Functional Information from GO Data
ChainGOidnamespacecontents
A0008239molecular_functiondipeptidyl-peptidase activity
A0070009molecular_functionserine-type aminopeptidase activity
B0008239molecular_functiondipeptidyl-peptidase activity
B0070009molecular_functionserine-type aminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue GOL A 801
ChainResidue
AARG391
ATRP395
AASP546

site_idAC2
Number of Residues13
Detailsbinding site for residue C8O A 802
ChainResidue
AASN654
ASER655
AASN670
APHE671
AASP672
AARG673
AHOH901
AHIS85
AASN218
ATRP219
ATHR650
ATHR651
AGLY652

site_idAC3
Number of Residues11
Detailsbinding site for residue C8O B 801
ChainResidue
BASN218
BTRP219
BTHR650
BTHR651
BGLY652
BASN654
BSER655
BASN670
BPHE671
BASP672
BARG673

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Charge relay system","evidences":[{"source":"UniProtKB","id":"V5YM14","evidenceCode":"ECO:0000250"},{"source":"PubMed","id":"26057589","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive 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"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsSite: {"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"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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