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5JM9

Structure of S. cerevesiae mApe1 dodecamer

Functional Information from GO Data
ChainGOidnamespacecontents
A0000324cellular_componentfungal-type vacuole
A0004177molecular_functionaminopeptidase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005773cellular_componentvacuole
A0006508biological_processproteolysis
A0008237molecular_functionmetallopeptidase activity
A0008270molecular_functionzinc ion binding
A0015031biological_processprotein transport
A0032258biological_processcytoplasm to vacuole targeting by the Cvt pathway
A0034270cellular_componentCvt complex
A0042802molecular_functionidentical protein binding
A0046872molecular_functionmetal ion binding
A0070006molecular_functionmetalloaminopeptidase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q9ULA0
ChainResidueDetails
AHIS88
AHIS166
AASP259
AGLU295
AGLU296
AASP341
AHIS344
AHIS435

site_idSWS_FT_FI2
Number of Residues1
DetailsSITE: Cleavage; by protease B (PrB/PRB1) => ECO:0000269|PubMed:1400574
ChainResidueDetails
ALEU1

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ASER312

site_idSWS_FT_FI4
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN63
AASN66
AASN404

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PDB entries from 2024-07-24

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