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2BKL

Structural and Mechanistic Analysis of Two Prolyl Endopeptidases: Role of Inter-Domain Dynamics in Catalysis and Specificity

Functional Information from GO Data
ChainGOidnamespacecontents
A0004252molecular_functionserine-type endopeptidase activity
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008236molecular_functionserine-type peptidase activity
A0016787molecular_functionhydrolase activity
A0070012molecular_functionoligopeptidase activity
B0004252molecular_functionserine-type endopeptidase activity
B0005829cellular_componentcytosol
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008236molecular_functionserine-type peptidase activity
B0016787molecular_functionhydrolase activity
B0070012molecular_functionoligopeptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A1680
ChainResidue
ATHR176
APRO177
AASP178
AHOH2675
AHOH2676

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ZAH A1533
ChainResidue
APHE456
ASER533
AASN534
ATRP574
AARG618
AHIS651
AHOH2671
AHOH2672
ALYS169
ATYR170
ATRP249
ATYR453

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MES A1678
ChainResidue
AVAL20
AALA21
AHIS591
AHIS597
AVAL599
AARG600
APRO601
AHOH2054
AHOH2673
AHOH2674

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE MES A1679
ChainResidue
ATYR183
ATHR217
AVAL219
ALEU241
ALYS257
APRO259
AGLY260
AHOH2346

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ZAH B1533
ChainResidue
BTRP249
BTYR453
BPHE456
BSER533
BASN534
BTRP574
BARG618
BHIS651
BHOH2691
BHOH2692

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE ZAH B1679
ChainResidue
AASN79
ALYS133
AHOH2139
BVAL72
BTYR84
BARG99
BGLU102
BTRP403
BHOH2178
BHOH2693

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MES B1680
ChainResidue
BVAL20
BALA21
BHIS591
BHIS597
BVAL599
BARG600
BHOH2042
BHOH2628
BHOH2694
BHOH2695

Functional Information from PROSITE/UniProt
site_idPS00708
Number of Residues31
DetailsPRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DfhaAaeyLvqqkytqpkrlaiyGgSnGGLL
ChainResidueDetails
AASP508-LEU538

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pfq
ChainResidueDetails
ASER533
AASP616
AHIS651

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1pfq
ChainResidueDetails
BSER533
BASP616
BHIS651

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PDB entries from 2025-07-02

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