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1IU8

The X-ray Crystal Structure of Pyrrolidone-Carboxylate Peptidase from Hyperthermophilic Archaeon Pyrococcus horikoshii

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008234molecular_functioncysteine-type peptidase activity
A0016787molecular_functionhydrolase activity
A0016920molecular_functionpyroglutamyl-peptidase activity
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008234molecular_functioncysteine-type peptidase activity
B0016787molecular_functionhydrolase activity
B0016920molecular_functionpyroglutamyl-peptidase activity
Functional Information from PROSITE/UniProt
site_idPS01333
Number of Residues17
DetailsPYRASE_GLU Pyrrolidone-carboxylate peptidase glutamic acid active site. GlaPgrthISvERVAvN
ChainResidueDetails
AGLY65-ASN81

site_idPS01334
Number of Residues15
DetailsPYRASE_CYS Pyrrolidone-carboxylate peptidase cysteine active site. IpAvLSyTAGtYLCN
ChainResidueDetails
AILE126-ASN140

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1aug
ChainResidueDetails
AGLU76
ACYS139
AARG86
AHIS163

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1aug
ChainResidueDetails
BGLU76
BCYS139
BARG86
BHIS163

246704

PDB entries from 2025-12-24

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