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4Y02

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0008239molecular_functiondipeptidyl-peptidase activity
A0070009molecular_functionserine-type aminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue GOL A 801
ChainResidue
AASP60
APHE124
ALYS194
APRO253
ALYS254
AARG255
AHOH999

site_idAC2
Number of Residues3
Detailsbinding site for residue GOL A 802
ChainResidue
AHOH904
ATHR195
ATHR197

site_idAC3
Number of Residues5
Detailsbinding site for residue K A 803
ChainResidue
ATHR278
ATHR651
AASP681
AHOH995
AHOH1331

site_idAC4
Number of Residues5
Detailsbinding site for residue K A 804
ChainResidue
AASN218
ATRP219
AASP672
AHOH966
AHOH1316

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000250|UniProtKB:V5YM14, ECO:0000305|PubMed:26057589
ChainResidueDetails
AHIS85
AASP227

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Charge relay system => ECO:0000250|UniProtKB:V5YM14, ECO:0000305|PubMed:21896480, ECO:0000305|PubMed:26057589
ChainResidueDetails
ASER655

site_idSWS_FT_FI3
Number of Residues1
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

218853

PDB entries from 2024-04-24

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