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1YR2

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
A0006508biological_processproteolysis
A0008236molecular_functionserine-type peptidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 750
ChainResidue
APRO589
AASP590
APHE592
ATYR647
APRO648
ALYS681
AHOH1304
AHOH1310

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 755
ChainResidue
AALA197
AGLY644
AVAL645
AASP646
AALA677
AHOH792
AHOH878
AHOH934
AARG175

Functional Information from PROSITE/UniProt
site_idPS00708
Number of Residues31
DetailsPRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DfiaAgewLiangvtprhglaieGgSnGGLL
ChainResidueDetails
AASP550-LEU580

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1pfq
ChainResidueDetails
ASER575
AASP658

224572

PDB entries from 2024-09-04

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