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1XRR

Crystal structure of active site F1-mutant E245Q soaked with peptide Pro-Pro

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016020cellular_componentmembrane
A0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PRO A 300
ChainResidue
AGLY37
ASER105
ATYR106
AASN209
AGLU213
AILE216
AGLN245

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PRO A 301
ChainResidue
ATYR205
APRO211
AASN212
AVAL174
ATYR178

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
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
ASER105
AHIS271
AASP244

239149

PDB entries from 2025-07-23

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