5JH9
Crystal structure of prApe1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000324 | cellular_component | fungal-type vacuole |
| A | 0004177 | molecular_function | aminopeptidase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005773 | cellular_component | vacuole |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0015031 | biological_process | protein transport |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0032258 | biological_process | cytoplasm to vacuole targeting by the Cvt pathway |
| A | 0034270 | cellular_component | Cvt complex |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070006 | molecular_function | metalloaminopeptidase activity |
| B | 0000324 | cellular_component | fungal-type vacuole |
| B | 0004177 | molecular_function | aminopeptidase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005773 | cellular_component | vacuole |
| B | 0006508 | biological_process | proteolysis |
| B | 0008233 | molecular_function | peptidase activity |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0015031 | biological_process | protein transport |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0032258 | biological_process | cytoplasm to vacuole targeting by the Cvt pathway |
| B | 0034270 | cellular_component | Cvt complex |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0070006 | molecular_function | metalloaminopeptidase activity |
| C | 0000324 | cellular_component | fungal-type vacuole |
| C | 0004177 | molecular_function | aminopeptidase activity |
| C | 0005515 | molecular_function | protein binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005773 | cellular_component | vacuole |
| C | 0006508 | biological_process | proteolysis |
| C | 0008233 | molecular_function | peptidase activity |
| C | 0008237 | molecular_function | metallopeptidase activity |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0015031 | biological_process | protein transport |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0032258 | biological_process | cytoplasm to vacuole targeting by the Cvt pathway |
| C | 0034270 | cellular_component | Cvt complex |
| C | 0042802 | molecular_function | identical protein binding |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0070006 | molecular_function | metalloaminopeptidase activity |
| D | 0000324 | cellular_component | fungal-type vacuole |
| D | 0004177 | molecular_function | aminopeptidase activity |
| D | 0005515 | molecular_function | protein binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005773 | cellular_component | vacuole |
| D | 0006508 | biological_process | proteolysis |
| D | 0008233 | molecular_function | peptidase activity |
| D | 0008237 | molecular_function | metallopeptidase activity |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0015031 | biological_process | protein transport |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0032258 | biological_process | cytoplasm to vacuole targeting by the Cvt pathway |
| D | 0034270 | cellular_component | Cvt complex |
| D | 0042802 | molecular_function | identical protein binding |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0070006 | molecular_function | metalloaminopeptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue ZN A 601 |
| Chain | Residue |
| A | HIS132 |
| A | ASP303 |
| A | ASP385 |
| A | ZN602 |
| A | CAC603 |
| A | HOH765 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN A 602 |
| Chain | Residue |
| A | ZN601 |
| A | CAC603 |
| A | ASP303 |
| A | GLU340 |
| A | HIS479 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue CAC A 603 |
| Chain | Residue |
| A | HIS132 |
| A | ASP303 |
| A | GLU339 |
| A | GLU340 |
| A | ASP385 |
| A | GLY454 |
| A | HIS479 |
| A | ZN601 |
| A | ZN602 |
| B | HIS210 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue CAC A 604 |
| Chain | Residue |
| A | PRO214 |
| A | GLU216 |
| A | PRO218 |
| A | PHE219 |
| A | GLN224 |
| B | HOH747 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue ZN B 601 |
| Chain | Residue |
| B | HIS132 |
| B | ASP303 |
| B | ASP385 |
| B | ZN602 |
| B | CAC603 |
| B | HOH852 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 602 |
| Chain | Residue |
| B | ASP303 |
| B | GLU340 |
| B | HIS479 |
| B | ZN601 |
| B | CAC603 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | binding site for residue CAC B 603 |
| Chain | Residue |
| A | HIS210 |
| B | HIS132 |
| B | ASP303 |
| B | GLU339 |
| B | GLU340 |
| B | ASP385 |
| B | GLY454 |
| B | HIS479 |
| B | ZN601 |
| B | ZN602 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue CAC B 604 |
| Chain | Residue |
| A | HOH741 |
| B | LYS213 |
| B | PRO214 |
| B | GLU216 |
| B | PRO218 |
| B | PHE219 |
| B | GLN224 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | binding site for residue ZN C 601 |
| Chain | Residue |
| C | HIS132 |
| C | ASP303 |
| C | ASP385 |
| C | ZN602 |
| C | CAC603 |
| C | HOH861 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue ZN C 602 |
| Chain | Residue |
| C | ASP303 |
| C | GLU340 |
| C | HIS479 |
| C | ZN601 |
| C | CAC603 |
| site_id | AD2 |
| Number of Residues | 10 |
| Details | binding site for residue CAC C 603 |
| Chain | Residue |
| C | HIS132 |
| C | ASP303 |
| C | GLU339 |
| C | GLU340 |
| C | ASP385 |
| C | GLY454 |
| C | HIS479 |
| C | ZN601 |
| C | ZN602 |
| D | HIS210 |
| site_id | AD3 |
| Number of Residues | 7 |
| Details | binding site for residue CAC C 604 |
| Chain | Residue |
| C | LYS213 |
| C | PRO214 |
| C | GLU216 |
| C | PRO218 |
| C | PHE219 |
| C | GLN224 |
| D | HOH766 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue ZN D 601 |
| Chain | Residue |
| D | HIS132 |
| D | ASP303 |
| D | ASP385 |
| D | ZN602 |
| D | CAC603 |
| D | HOH829 |
| site_id | AD5 |
| Number of Residues | 5 |
| Details | binding site for residue ZN D 602 |
| Chain | Residue |
| D | ASP303 |
| D | GLU340 |
| D | HIS479 |
| D | ZN601 |
| D | CAC603 |
| site_id | AD6 |
| Number of Residues | 10 |
| Details | binding site for residue CAC D 603 |
| Chain | Residue |
| D | ASP385 |
| D | GLY454 |
| D | HIS479 |
| D | ZN601 |
| D | ZN602 |
| C | HIS210 |
| D | HIS132 |
| D | ASP303 |
| D | GLU339 |
| D | GLU340 |
| site_id | AD7 |
| Number of Residues | 6 |
| Details | binding site for residue CAC D 604 |
| Chain | Residue |
| C | HOH804 |
| D | PRO214 |
| D | GLU216 |
| D | PRO218 |
| D | PHE219 |
| D | GLN224 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"5JGF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5JH9","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9ULA0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"5JGF","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Site: {"description":"Cleavage; by protease B (PrB/PRB1)","evidences":[{"source":"PubMed","id":"1400574","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
