Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4Y01

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

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 Residues1
Detailsbinding site for residue GOL A 801
ChainResidue
AASP546

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

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon