7SRV
Metal dependent activation of Plasmodium falciparum M17 aminopeptidase (inactive form), spacegroup P22121
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0006508 | biological_process | proteolysis |
A | 0019538 | biological_process | protein metabolic process |
A | 0030145 | molecular_function | manganese ion binding |
A | 0046872 | molecular_function | metal ion binding |
A | 0070006 | molecular_function | metalloaminopeptidase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0006508 | biological_process | proteolysis |
B | 0019538 | biological_process | protein metabolic process |
B | 0030145 | molecular_function | manganese ion binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0070006 | molecular_function | metalloaminopeptidase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0006508 | biological_process | proteolysis |
C | 0019538 | biological_process | protein metabolic process |
C | 0030145 | molecular_function | manganese ion binding |
C | 0046872 | molecular_function | metal ion binding |
C | 0070006 | molecular_function | metalloaminopeptidase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0006508 | biological_process | proteolysis |
D | 0019538 | biological_process | protein metabolic process |
D | 0030145 | molecular_function | manganese ion binding |
D | 0046872 | molecular_function | metal ion binding |
D | 0070006 | molecular_function | metalloaminopeptidase activity |
E | 0005737 | cellular_component | cytoplasm |
E | 0006508 | biological_process | proteolysis |
E | 0019538 | biological_process | protein metabolic process |
E | 0030145 | molecular_function | manganese ion binding |
E | 0046872 | molecular_function | metal ion binding |
E | 0070006 | molecular_function | metalloaminopeptidase activity |
F | 0005737 | cellular_component | cytoplasm |
F | 0006508 | biological_process | proteolysis |
F | 0019538 | biological_process | protein metabolic process |
F | 0030145 | molecular_function | manganese ion binding |
F | 0046872 | molecular_function | metal ion binding |
F | 0070006 | molecular_function | metalloaminopeptidase activity |
Functional Information from PROSITE/UniProt
site_id | PS00631 |
Number of Residues | 8 |
Details | CYTOSOL_AP Cytosol aminopeptidase signature. NTDAEGRL |
Chain | Residue | Details |
A | ASN457-LEU464 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P00727 |
Chain | Residue | Details |
A | LYS386 | |
E | ARG463 | |
F | LYS386 | |
F | ARG463 | |
A | ARG463 | |
B | LYS386 | |
B | ARG463 | |
C | LYS386 | |
C | ARG463 | |
D | LYS386 | |
D | ARG463 | |
E | LYS386 |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20133789, ECO:0000269|PubMed:21844374, ECO:0000269|PubMed:23713488, ECO:0000269|PubMed:25299353, ECO:0000269|PubMed:25645579, ECO:0000269|PubMed:35691342, ECO:0000269|Ref.13, ECO:0000312|PDB:3T8W, ECO:0007744|PDB:3KQX, ECO:0007744|PDB:3KQZ, ECO:0007744|PDB:3KR4, ECO:0007744|PDB:3KR5, ECO:0007744|PDB:4K3N, ECO:0007744|PDB:4R6T, ECO:0007744|PDB:4R76, ECO:0007744|PDB:4R7M, ECO:0007744|PDB:4X2T, ECO:0007744|PDB:7RIE, ECO:0007744|PDB:7T3V |
Chain | Residue | Details |
A | LYS374 | |
D | LYS374 | |
D | ASP379 | |
D | GLU461 | |
E | LYS374 | |
E | ASP379 | |
E | GLU461 | |
F | LYS374 | |
F | ASP379 | |
F | GLU461 | |
A | ASP379 | |
A | GLU461 | |
B | LYS374 | |
B | ASP379 | |
B | GLU461 | |
C | LYS374 | |
C | ASP379 | |
C | GLU461 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000305|PubMed:20133789, ECO:0000305|PubMed:23713488, ECO:0007744|PDB:3KR5, ECO:0007744|PDB:4K3N |
Chain | Residue | Details |
A | LYS386 | |
B | LYS386 | |
C | LYS386 | |
D | LYS386 | |
E | LYS386 | |
F | LYS386 |
site_id | SWS_FT_FI4 |
Number of Residues | 18 |
Details | BINDING: BINDING => ECO:0000269|PubMed:35691342, ECO:0007744|PDB:7SRV |
Chain | Residue | Details |
A | ASP394 | |
D | ASP394 | |
D | MET396 | |
D | ASP399 | |
E | ASP394 | |
E | MET396 | |
E | ASP399 | |
F | ASP394 | |
F | MET396 | |
F | ASP399 | |
A | MET396 | |
A | ASP399 | |
B | ASP394 | |
B | MET396 | |
B | ASP399 | |
C | ASP394 | |
C | MET396 | |
C | ASP399 |
site_id | SWS_FT_FI5 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:20133789, ECO:0000269|PubMed:21844374, ECO:0000269|PubMed:23713488, ECO:0000269|PubMed:25299353, ECO:0000269|PubMed:25645579, ECO:0000269|PubMed:35691342, ECO:0000269|Ref.13, ECO:0000312|PDB:3KQZ, ECO:0000312|PDB:3T8W, ECO:0007744|PDB:3KR4, ECO:0007744|PDB:3KR5, ECO:0007744|PDB:4K3N, ECO:0007744|PDB:4R6T, ECO:0007744|PDB:4R76, ECO:0007744|PDB:4R7M, ECO:0007744|PDB:4X2T, ECO:0007744|PDB:7RIE, ECO:0007744|PDB:7T3V |
Chain | Residue | Details |
A | ASP459 | |
B | ASP459 | |
C | ASP459 | |
D | ASP459 | |
E | ASP459 | |
F | ASP459 |
site_id | SWS_FT_FI6 |
Number of Residues | 6 |
Details | SITE: Essential for hexamer stabilization => ECO:0000269|PubMed:35691342 |
Chain | Residue | Details |
A | LYS386 | |
B | LYS386 | |
C | LYS386 | |
D | LYS386 | |
E | LYS386 | |
F | LYS386 |