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5WDL

A processive dipeptidyl aminopeptidase secreted from an established commensal bacterium P. distasonis

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0005737cellular_componentcytoplasm
A0006508biological_processproteolysis
A0008234molecular_functioncysteine-type peptidase activity
A0009401biological_processphosphoenolpyruvate-dependent sugar phosphotransferase system
A0009636biological_processresponse to toxic substance
A0016020cellular_componentmembrane
A0043418biological_processhomocysteine catabolic process
A0046872molecular_functionmetal ion binding
A0070005molecular_functioncysteine-type aminopeptidase activity
B0004177molecular_functionaminopeptidase activity
B0005737cellular_componentcytoplasm
B0006508biological_processproteolysis
B0008234molecular_functioncysteine-type peptidase activity
B0009401biological_processphosphoenolpyruvate-dependent sugar phosphotransferase system
B0009636biological_processresponse to toxic substance
B0016020cellular_componentmembrane
B0043418biological_processhomocysteine catabolic process
B0046872molecular_functionmetal ion binding
B0070005molecular_functioncysteine-type aminopeptidase activity
C0004177molecular_functionaminopeptidase activity
C0005737cellular_componentcytoplasm
C0006508biological_processproteolysis
C0008234molecular_functioncysteine-type peptidase activity
C0009401biological_processphosphoenolpyruvate-dependent sugar phosphotransferase system
C0009636biological_processresponse to toxic substance
C0016020cellular_componentmembrane
C0043418biological_processhomocysteine catabolic process
C0046872molecular_functionmetal ion binding
C0070005molecular_functioncysteine-type aminopeptidase activity
D0004177molecular_functionaminopeptidase activity
D0005737cellular_componentcytoplasm
D0006508biological_processproteolysis
D0008234molecular_functioncysteine-type peptidase activity
D0009401biological_processphosphoenolpyruvate-dependent sugar phosphotransferase system
D0009636biological_processresponse to toxic substance
D0016020cellular_componentmembrane
D0043418biological_processhomocysteine catabolic process
D0046872molecular_functionmetal ion binding
D0070005molecular_functioncysteine-type aminopeptidase activity
E0004177molecular_functionaminopeptidase activity
E0005737cellular_componentcytoplasm
E0006508biological_processproteolysis
E0008234molecular_functioncysteine-type peptidase activity
E0009401biological_processphosphoenolpyruvate-dependent sugar phosphotransferase system
E0009636biological_processresponse to toxic substance
E0016020cellular_componentmembrane
E0043418biological_processhomocysteine catabolic process
E0046872molecular_functionmetal ion binding
E0070005molecular_functioncysteine-type aminopeptidase activity
F0004177molecular_functionaminopeptidase activity
F0005737cellular_componentcytoplasm
F0006508biological_processproteolysis
F0008234molecular_functioncysteine-type peptidase activity
F0009401biological_processphosphoenolpyruvate-dependent sugar phosphotransferase system
F0009636biological_processresponse to toxic substance
F0016020cellular_componentmembrane
F0043418biological_processhomocysteine catabolic process
F0046872molecular_functionmetal ion binding
F0070005molecular_functioncysteine-type aminopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues11
Detailsbinding site for residue R33 A 501
ChainResidue
AGLN50
AASP339
AHIS340
AGLY54
ATHR55
ACYS56
ATRP57
AGLY108
AGLY109
AASP237
AASP338

site_idAC2
Number of Residues5
Detailsbinding site for residue K A 502
ChainResidue
AASP78
ALEU79
AGLU81
AGLU126
AHOH702

site_idAC3
Number of Residues6
Detailsbinding site for residue K A 503
ChainResidue
AASP271
ASER273
AGLU274
AGLU335
AHOH679
AHOH704

site_idAC4
Number of Residues6
Detailsbinding site for residue K B 502
ChainResidue
BASP78
BLEU79
BGLU81
BGLU126
BHOH602
BHOH694

site_idAC5
Number of Residues6
Detailsbinding site for residue K B 503
ChainResidue
BASP271
BSER273
BGLU274
BGLU335
BHOH632
BHOH699

site_idAC6
Number of Residues6
Detailsbinding site for residue K C 502
ChainResidue
CASP78
CLEU79
CGLU81
CGLU126
CHOH609
CHOH673

site_idAC7
Number of Residues6
Detailsbinding site for residue K C 503
ChainResidue
CASP271
CSER273
CGLU274
CGLU335
CHOH606
CHOH678

site_idAC8
Number of Residues5
Detailsbinding site for residue K D 502
ChainResidue
DASP78
DLEU79
DGLU81
DGLU126
DHOH645

site_idAC9
Number of Residues6
Detailsbinding site for residue K D 503
ChainResidue
DASP271
DSER273
DGLU274
DGLU335
DHOH658
DHOH710

site_idAD1
Number of Residues6
Detailsbinding site for residue K E 502
ChainResidue
EASP78
ELEU79
EGLU81
EGLU126
EHOH612
EHOH754

site_idAD2
Number of Residues6
Detailsbinding site for residue K E 503
ChainResidue
EASP271
ESER273
EGLU274
EGLU335
EHOH692
EHOH750

site_idAD3
Number of Residues6
Detailsbinding site for residue K F 502
ChainResidue
FASP78
FLEU79
FGLU81
FGLU126
FHOH605
FHOH773

site_idAD4
Number of Residues6
Detailsbinding site for residue K F 503
ChainResidue
FASP271
FSER273
FGLU274
FGLU335
FHOH733
FHOH777

site_idAD5
Number of Residues15
Detailsbinding site for Di-peptide R33 B 501 and CYS B 56
ChainResidue
BGLN50
BGLY54
BTHR55
BTRP57
BCYS58
BTYR59
BSER60
BSER106
BGLY108
BGLY109
BASP237
BASP338
BASP339
BHIS340
BGLY341

site_idAD6
Number of Residues16
Detailsbinding site for Di-peptide R33 C 501 and CYS C 56
ChainResidue
CTRP57
CCYS58
CTYR59
CSER60
CSER106
CGLN107
CGLY108
CGLY109
CASP237
CASP338
CASP339
CHIS340
CGLY341
CGLN50
CGLY54
CTHR55

site_idAD7
Number of Residues16
Detailsbinding site for Di-peptide R33 D 501 and CYS D 56
ChainResidue
DGLN50
DGLY54
DTHR55
DTRP57
DCYS58
DTYR59
DSER60
DGLY108
DGLY109
DASP237
DASP338
DASP339
DHIS340
DGLY341
DHOH607
DHOH695

site_idAD8
Number of Residues16
Detailsbinding site for Di-peptide R33 E 501 and CYS E 56
ChainResidue
EGLN50
EGLY54
ETHR55
ETRP57
ECYS58
ETYR59
ESER60
ESER106
EGLY108
EGLY109
EASP237
EASP338
EASP339
EHIS340
EGLY341
EHOH603

site_idAD9
Number of Residues15
Detailsbinding site for Di-peptide R33 F 501 and CYS F 56
ChainResidue
FGLN50
FGLY54
FTHR55
FTRP57
FCYS58
FTYR59
FSER60
FGLY108
FGLY109
FASP237
FASP338
FASP339
FHIS340
FGLY341
FHOH608

Functional Information from PROSITE/UniProt
site_idPS00139
Number of Residues12
DetailsTHIOL_PROTEASE_CYS Eukaryotic thiol (cysteine) proteases cysteine active site. QNrAGTCWCySS
ChainResidueDetails
AGLN50-SER61

222624

PDB entries from 2024-07-17

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