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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
DetailsACT_SITE: Charge relay system => ECO:0000250|UniProtKB:V5YM14, ECO:0000305|PubMed:26057589
ChainResidueDetails
AHIS85
AASP227
BHIS85
BASP227

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000250|UniProtKB:V5YM14, ECO:0000305|PubMed:21896480, ECO:0000305|PubMed:26057589
ChainResidueDetails
ASER655
BSER655

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: 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
ChainResidueDetails
AARG673
BARG673

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PDB entries from 2024-07-17

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