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1X2E

The crystal structure of prolyl aminopeptidase complexed with Ala-TBODA

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0005737cellular_componentcytoplasm
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE ATX A 401
ChainResidue
AGLY45
AGLY46
ASER113
ATRP114
AARG136
APHE139
AGLU204
AGLU232
AHIS296

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues255
DetailsDomain: {"description":"AB hydrolase-1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Nucleophile"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Proton donor"}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1azw
ChainResidueDetails
ASER113
AASP268
AHIS296

242500

PDB entries from 2025-10-01

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