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5JWI

Crystal structure of Porphyromonas endodontalis DPP11 in complex with dipeptide Arg-Glu

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0005576cellular_componentextracellular region
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
A0008239molecular_functiondipeptidyl-peptidase activity
A0009986cellular_componentcell surface
A0043171biological_processpeptide catabolic process
A0070009molecular_functionserine-type aminopeptidase activity
B0004177molecular_functionaminopeptidase activity
B0005576cellular_componentextracellular region
B0006508biological_processproteolysis
B0008236molecular_functionserine-type peptidase activity
B0008239molecular_functiondipeptidyl-peptidase activity
B0009986cellular_componentcell surface
B0043171biological_processpeptide catabolic process
B0070009molecular_functionserine-type aminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue ARG A 801
ChainResidue
AHIS85
AGLU802
AHOH1071
AHOH1079
AHOH1134
ASER213
AASN217
ATRP218
AALA328
AGLN331
AASN332
APHE668
AASP669

site_idAC2
Number of Residues11
Detailsbinding site for residue GLU A 802
ChainResidue
AHIS85
ATHR647
ATHR648
AGLY649
AGLY650
AALA652
AASN667
APHE668
AASP669
AARG670
AARG801

site_idAC3
Number of Residues4
Detailsbinding site for residue CL B 801
ChainResidue
BVAL263
BLYS595
BASN632
BARG694

site_idAC4
Number of Residues3
Detailsbinding site for residue CL B 802
ChainResidue
BLEU682
BPRO683
BASN684

site_idAC5
Number of Residues7
Detailsbinding site for residue ARG B 803
ChainResidue
BSER213
BASN217
BTRP218
BALA328
BASN332
BASP669
BGLU804

site_idAC6
Number of Residues12
Detailsbinding site for residue GLU B 804
ChainResidue
BHIS85
BTHR647
BTHR648
BGLY649
BGLY650
BASN651
BALA652
BASN667
BPHE668
BASP669
BARG670
BARG803

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Charge relay system => ECO:0000250|UniProtKB:V5YM14
ChainResidueDetails
AHIS85
AASP226
BHIS85
BASP226

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000250|UniProtKB:V5YM14, ECO:0000305|PubMed:21896480
ChainResidueDetails
AALA652
BALA652

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:0000250|UniProtKB:B2RID1, ECO:0000305|PubMed:21896480
ChainResidueDetails
AARG670
BARG670

222036

PDB entries from 2024-07-03

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