4R7M
Structure of the m17 leucyl aminopeptidase from malaria complexed with a hydroxamic acid-based inhibitor
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 |
| G | 0005737 | cellular_component | cytoplasm |
| G | 0006508 | biological_process | proteolysis |
| G | 0019538 | biological_process | protein metabolic process |
| G | 0030145 | molecular_function | manganese ion binding |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0070006 | molecular_function | metalloaminopeptidase activity |
| H | 0005737 | cellular_component | cytoplasm |
| H | 0006508 | biological_process | proteolysis |
| H | 0019538 | biological_process | protein metabolic process |
| H | 0030145 | molecular_function | manganese ion binding |
| H | 0046872 | molecular_function | metal ion binding |
| H | 0070006 | molecular_function | metalloaminopeptidase activity |
| I | 0005737 | cellular_component | cytoplasm |
| I | 0006508 | biological_process | proteolysis |
| I | 0019538 | biological_process | protein metabolic process |
| I | 0030145 | molecular_function | manganese ion binding |
| I | 0046872 | molecular_function | metal ion binding |
| I | 0070006 | molecular_function | metalloaminopeptidase activity |
| J | 0005737 | cellular_component | cytoplasm |
| J | 0006508 | biological_process | proteolysis |
| J | 0019538 | biological_process | protein metabolic process |
| J | 0030145 | molecular_function | manganese ion binding |
| J | 0046872 | molecular_function | metal ion binding |
| J | 0070006 | molecular_function | metalloaminopeptidase activity |
| K | 0005737 | cellular_component | cytoplasm |
| K | 0006508 | biological_process | proteolysis |
| K | 0019538 | biological_process | protein metabolic process |
| K | 0030145 | molecular_function | manganese ion binding |
| K | 0046872 | molecular_function | metal ion binding |
| K | 0070006 | molecular_function | metalloaminopeptidase activity |
| L | 0005737 | cellular_component | cytoplasm |
| L | 0006508 | biological_process | proteolysis |
| L | 0019538 | biological_process | protein metabolic process |
| L | 0030145 | molecular_function | manganese ion binding |
| L | 0046872 | molecular_function | metal ion binding |
| L | 0070006 | molecular_function | metalloaminopeptidase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 1001 |
| Chain | Residue |
| A | LYS374 |
| A | ASP379 |
| A | ASP399 |
| A | GLU461 |
| A | ZN1003 |
| A | 3MW1006 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO3 A 1002 |
| Chain | Residue |
| A | ARG463 |
| A | LEU487 |
| A | 3MW1006 |
| A | LYS374 |
| A | ALA460 |
| A | GLY462 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 1003 |
| Chain | Residue |
| A | ASP379 |
| A | LYS386 |
| A | ASP459 |
| A | GLU461 |
| A | ZN1001 |
| A | 3MW1006 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE 1PE A 1004 |
| Chain | Residue |
| A | ALA388 |
| A | PRO389 |
| A | GLY489 |
| A | 3MW1006 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE 1PE A 1005 |
| Chain | Residue |
| A | TYR103 |
| A | HIS108 |
| A | TYR411 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 3MW A 1006 |
| Chain | Residue |
| A | LYS374 |
| A | ASP379 |
| A | LYS386 |
| A | MET392 |
| A | MET396 |
| A | ASP399 |
| A | ASN457 |
| A | ASP459 |
| A | GLU461 |
| A | LEU487 |
| A | THR488 |
| A | GLY489 |
| A | LEU492 |
| A | ZN1001 |
| A | CO31002 |
| A | ZN1003 |
| A | 1PE1004 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 1001 |
| Chain | Residue |
| B | LYS374 |
| B | ASP379 |
| B | ASP399 |
| B | GLU461 |
| B | ZN1003 |
| B | 3MW1005 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO3 B 1002 |
| Chain | Residue |
| B | LYS374 |
| B | ALA460 |
| B | GLY462 |
| B | ARG463 |
| B | LEU487 |
| B | 3MW1005 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 1003 |
| Chain | Residue |
| B | ASP379 |
| B | ASP459 |
| B | GLU461 |
| B | ZN1001 |
| B | 3MW1005 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1004 |
| Chain | Residue |
| A | SER435 |
| A | LYS436 |
| B | SER435 |
| B | LYS436 |
| C | SER435 |
| C | LYS436 |
| site_id | BC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 3MW B 1005 |
| Chain | Residue |
| B | LYS374 |
| B | ASP379 |
| B | LYS386 |
| B | MET392 |
| B | PHE398 |
| B | ASN457 |
| B | ASP459 |
| B | GLU461 |
| B | LEU487 |
| B | THR488 |
| B | GLY489 |
| B | ZN1001 |
| B | CO31002 |
| B | ZN1003 |
| B | HOH1111 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN C 1001 |
| Chain | Residue |
| C | LYS374 |
| C | ASP379 |
| C | ASP399 |
| C | GLU461 |
| C | ZN1003 |
| C | 3MW1007 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO3 C 1002 |
| Chain | Residue |
| C | LYS374 |
| C | GLY462 |
| C | ARG463 |
| C | LEU487 |
| C | 3MW1007 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 1003 |
| Chain | Residue |
| C | ASP379 |
| C | ASP459 |
| C | GLU461 |
| C | ZN1001 |
| C | 3MW1007 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 1004 |
| Chain | Residue |
| C | GLY126 |
| C | LEU219 |
| C | SER220 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 1PE C 1005 |
| Chain | Residue |
| C | TYR103 |
| C | HIS108 |
| C | PHE289 |
| C | LYS320 |
| C | LEU321 |
| C | TYR411 |
| site_id | BC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE 1PE C 1006 |
| Chain | Residue |
| C | ILE529 |
| C | ILE530 |
| C | ASN531 |
| C | GLU532 |
| D | GLU200 |
| D | ALA201 |
| D | SER498 |
| D | TYR499 |
| D | HOH1126 |
| site_id | BC9 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 3MW C 1007 |
| Chain | Residue |
| C | LYS374 |
| C | ASP379 |
| C | LYS386 |
| C | MET392 |
| C | ASP459 |
| C | GLU461 |
| C | LEU487 |
| C | THR488 |
| C | GLY489 |
| C | LEU492 |
| C | ALA577 |
| C | ZN1001 |
| C | CO31002 |
| C | ZN1003 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN D 1001 |
| Chain | Residue |
| D | LYS374 |
| D | ASP379 |
| D | ASP399 |
| D | GLU461 |
| D | ZN1003 |
| D | 3MW1004 |
| site_id | CC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CO3 D 1002 |
| Chain | Residue |
| D | LYS374 |
| D | ALA460 |
| D | GLU461 |
| D | GLY462 |
| D | ARG463 |
| D | LEU487 |
| D | 3MW1004 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 1003 |
| Chain | Residue |
| D | ASP379 |
| D | ASP459 |
| D | GLU461 |
| D | ZN1001 |
| D | 3MW1004 |
| site_id | CC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 3MW D 1004 |
| Chain | Residue |
| D | LYS374 |
| D | ASP379 |
| D | LYS386 |
| D | MET392 |
| D | ASP399 |
| D | ASN457 |
| D | ASP459 |
| D | GLU461 |
| D | LEU487 |
| D | THR488 |
| D | GLY489 |
| D | LEU492 |
| D | ALA577 |
| D | ZN1001 |
| D | CO31002 |
| D | ZN1003 |
| site_id | CC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN E 1001 |
| Chain | Residue |
| E | LYS374 |
| E | ASP379 |
| E | ASP399 |
| E | GLU461 |
| E | ZN1003 |
| E | 3MW1007 |
| site_id | CC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CO3 E 1002 |
| Chain | Residue |
| E | LYS374 |
| E | ALA460 |
| E | GLU461 |
| E | GLY462 |
| E | ARG463 |
| E | LEU487 |
| E | 3MW1007 |
| site_id | CC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN E 1003 |
| Chain | Residue |
| E | ASP379 |
| E | ASP459 |
| E | GLU461 |
| E | ZN1001 |
| E | 3MW1007 |
| site_id | CC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 E 1004 |
| Chain | Residue |
| D | SER435 |
| D | LYS436 |
| E | SER435 |
| E | LYS436 |
| F | SER435 |
| F | LYS436 |
| site_id | CC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 1PE E 1005 |
| Chain | Residue |
| E | TYR103 |
| E | ASN104 |
| E | HIS108 |
| E | PHE289 |
| E | LYS320 |
| E | TYR411 |
| site_id | DC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE 1PE E 1006 |
| Chain | Residue |
| E | TYR103 |
| E | LYS320 |
| site_id | DC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 3MW E 1007 |
| Chain | Residue |
| E | ASP379 |
| E | LYS386 |
| E | MET392 |
| E | PHE398 |
| E | ASP399 |
| E | ASP459 |
| E | GLU461 |
| E | LEU487 |
| E | THR488 |
| E | GLY489 |
| E | ALA577 |
| E | ZN1001 |
| E | CO31002 |
| E | ZN1003 |
| site_id | DC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN F 1001 |
| Chain | Residue |
| F | LYS374 |
| F | ASP379 |
| F | ASP399 |
| F | GLU461 |
| F | ZN1003 |
| F | 3MW1005 |
| site_id | DC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO3 F 1002 |
| Chain | Residue |
| F | LYS374 |
| F | ALA460 |
| F | GLY462 |
| F | ARG463 |
| F | LEU487 |
| F | 3MW1005 |
| site_id | DC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN F 1003 |
| Chain | Residue |
| F | ASP379 |
| F | ASP459 |
| F | GLU461 |
| F | ZN1001 |
| F | 3MW1005 |
| site_id | DC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE 1PE F 1004 |
| Chain | Residue |
| F | ASP95 |
| F | PRO96 |
| F | THR97 |
| site_id | DC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 3MW F 1005 |
| Chain | Residue |
| F | LYS374 |
| F | ASP379 |
| F | MET392 |
| F | ASP399 |
| F | ASP459 |
| F | GLU461 |
| F | LEU487 |
| F | THR488 |
| F | GLY489 |
| F | LEU492 |
| F | ILE547 |
| F | ZN1001 |
| F | CO31002 |
| F | ZN1003 |
| site_id | DC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN G 1001 |
| Chain | Residue |
| G | LYS374 |
| G | ASP379 |
| G | ASP399 |
| G | GLU461 |
| G | ZN1003 |
| G | 3MW1008 |
| site_id | DC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CO3 G 1002 |
| Chain | Residue |
| G | LYS374 |
| G | ALA460 |
| G | GLU461 |
| G | GLY462 |
| G | ARG463 |
| G | LEU487 |
| G | 3MW1008 |
| site_id | EC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN G 1003 |
| Chain | Residue |
| G | ASP379 |
| G | ASP459 |
| G | GLU461 |
| G | ZN1001 |
| G | 3MW1008 |
| site_id | EC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 G 1004 |
| Chain | Residue |
| G | SER435 |
| G | LYS436 |
| H | SER435 |
| H | LYS436 |
| I | SER435 |
| I | LYS436 |
| site_id | EC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 G 1005 |
| Chain | Residue |
| G | TYR244 |
| G | ASP249 |
| G | TYR292 |
| G | SER295 |
| G | LYS587 |
| I | TYR541 |
| site_id | EC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE 1PE G 1006 |
| Chain | Residue |
| G | TYR103 |
| G | ASN104 |
| G | HIS108 |
| G | LYS320 |
| G | TYR411 |
| G | 1PE1007 |
| site_id | EC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE 1PE G 1007 |
| Chain | Residue |
| G | TYR103 |
| G | ASN104 |
| G | GLU316 |
| G | LYS320 |
| G | 1PE1006 |
| site_id | EC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 3MW G 1008 |
| Chain | Residue |
| G | LYS374 |
| G | ASP379 |
| G | LYS386 |
| G | MET392 |
| G | MET396 |
| G | PHE398 |
| G | ASP459 |
| G | GLU461 |
| G | ARG463 |
| G | LEU487 |
| G | THR488 |
| G | GLY489 |
| G | SER554 |
| G | ALA577 |
| G | ZN1001 |
| G | CO31002 |
| G | ZN1003 |
| site_id | EC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN H 1001 |
| Chain | Residue |
| H | LYS374 |
| H | ASP379 |
| H | ASP399 |
| H | GLU461 |
| H | ZN1003 |
| H | 3MW1005 |
| site_id | EC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO3 H 1002 |
| Chain | Residue |
| H | LYS374 |
| H | ALA460 |
| H | GLY462 |
| H | ARG463 |
| H | LEU487 |
| H | 3MW1005 |
| site_id | EC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN H 1003 |
| Chain | Residue |
| H | ASP379 |
| H | ASP459 |
| H | GLU461 |
| H | ZN1001 |
| H | 3MW1005 |
| site_id | FC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE 1PE H 1004 |
| Chain | Residue |
| B | ASN104 |
| H | TYR103 |
| H | ASN104 |
| H | LYS320 |
| H | TYR411 |
| site_id | FC2 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 3MW H 1005 |
| Chain | Residue |
| H | LYS374 |
| H | ASP379 |
| H | LYS386 |
| H | MET392 |
| H | PHE398 |
| H | ASN457 |
| H | ASP459 |
| H | GLU461 |
| H | LEU487 |
| H | THR488 |
| H | GLY489 |
| H | ZN1001 |
| H | CO31002 |
| H | ZN1003 |
| site_id | FC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN I 1001 |
| Chain | Residue |
| I | LYS374 |
| I | ASP379 |
| I | ASP399 |
| I | GLU461 |
| I | ZN1003 |
| I | 3MW1004 |
| site_id | FC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CO3 I 1002 |
| Chain | Residue |
| I | LYS374 |
| I | ALA460 |
| I | GLU461 |
| I | GLY462 |
| I | ARG463 |
| I | LEU487 |
| I | 3MW1004 |
| site_id | FC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN I 1003 |
| Chain | Residue |
| I | ASP379 |
| I | ASP459 |
| I | GLU461 |
| I | ZN1001 |
| I | 3MW1004 |
| site_id | FC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 3MW I 1004 |
| Chain | Residue |
| I | LYS374 |
| I | ASP379 |
| I | LYS386 |
| I | MET392 |
| I | PHE398 |
| I | ASP399 |
| I | ASP459 |
| I | GLU461 |
| I | LEU487 |
| I | THR488 |
| I | GLY489 |
| I | SER554 |
| I | ZN1001 |
| I | CO31002 |
| I | ZN1003 |
| site_id | FC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN J 1001 |
| Chain | Residue |
| J | LYS374 |
| J | ASP379 |
| J | ASP399 |
| J | GLU461 |
| J | ZN1003 |
| J | 3MW1005 |
| site_id | FC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO3 J 1002 |
| Chain | Residue |
| J | LYS374 |
| J | ALA460 |
| J | GLY462 |
| J | ARG463 |
| J | LEU487 |
| J | 3MW1005 |
| site_id | FC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN J 1003 |
| Chain | Residue |
| J | ASP379 |
| J | LYS386 |
| J | ASP459 |
| J | GLU461 |
| J | ZN1001 |
| J | 3MW1005 |
| site_id | GC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 J 1004 |
| Chain | Residue |
| J | SER435 |
| J | LYS436 |
| K | SER435 |
| K | LYS436 |
| L | SER435 |
| L | LYS436 |
| site_id | GC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 3MW J 1005 |
| Chain | Residue |
| J | LYS374 |
| J | ASP379 |
| J | LYS386 |
| J | MET392 |
| J | PHE398 |
| J | ASN457 |
| J | ASP459 |
| J | GLU461 |
| J | LEU487 |
| J | THR488 |
| J | GLY489 |
| J | ALA577 |
| J | ZN1001 |
| J | CO31002 |
| J | ZN1003 |
| site_id | GC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN K 1001 |
| Chain | Residue |
| K | LYS374 |
| K | ASP379 |
| K | ASP399 |
| K | GLU461 |
| K | ZN1003 |
| K | 3MW1006 |
| site_id | GC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CO3 K 1002 |
| Chain | Residue |
| K | LYS374 |
| K | ALA460 |
| K | GLU461 |
| K | GLY462 |
| K | ARG463 |
| K | LEU487 |
| K | 3MW1006 |
| site_id | GC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN K 1003 |
| Chain | Residue |
| K | ASP379 |
| K | ASP459 |
| K | GLU461 |
| K | ZN1001 |
| K | 3MW1006 |
| site_id | GC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 K 1004 |
| Chain | Residue |
| K | TYR103 |
| K | ASN104 |
| site_id | GC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE 1PE K 1005 |
| Chain | Residue |
| K | TYR103 |
| K | HIS108 |
| K | PHE289 |
| K | LYS320 |
| K | TYR411 |
| site_id | GC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 3MW K 1006 |
| Chain | Residue |
| K | LYS374 |
| K | ASP379 |
| K | LYS386 |
| K | MET392 |
| K | PHE398 |
| K | ASN457 |
| K | ASP459 |
| K | GLU461 |
| K | LEU487 |
| K | THR488 |
| K | GLY489 |
| K | ZN1001 |
| K | CO31002 |
| K | ZN1003 |
| site_id | GC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DMS K 1007 |
| Chain | Residue |
| K | GLY390 |
| K | SER391 |
| K | MET392 |
| site_id | HC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN L 1001 |
| Chain | Residue |
| L | LYS374 |
| L | ASP379 |
| L | ASP399 |
| L | GLU461 |
| L | ZN1003 |
| L | 3MW1005 |
| site_id | HC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CO3 L 1002 |
| Chain | Residue |
| L | LYS374 |
| L | ALA460 |
| L | GLY462 |
| L | ARG463 |
| L | LEU487 |
| L | 3MW1005 |
| site_id | HC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN L 1003 |
| Chain | Residue |
| L | ASP379 |
| L | ASP459 |
| L | GLU461 |
| L | ZN1001 |
| L | 3MW1005 |
| site_id | HC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 L 1004 |
| Chain | Residue |
| L | GLU102 |
| L | TYR103 |
| L | ASN104 |
| site_id | HC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 3MW L 1005 |
| Chain | Residue |
| L | LYS374 |
| L | ASP379 |
| L | LYS386 |
| L | MET392 |
| L | PHE398 |
| L | ASN457 |
| L | ASP459 |
| L | GLU461 |
| L | LEU487 |
| L | THR488 |
| L | GLY489 |
| L | LEU492 |
| L | ZN1001 |
| L | CO31002 |
| L | ZN1003 |
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 | 24 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:P00727 |
| Chain | Residue | Details |
| A | LYS386 | |
| A | ARG463 | |
| B | LYS386 | |
| B | ARG463 | |
| C | LYS386 | |
| C | ARG463 | |
| D | LYS386 | |
| D | ARG463 | |
| E | LYS386 | |
| E | ARG463 | |
| F | LYS386 | |
| F | ARG463 | |
| G | LYS386 | |
| G | ARG463 | |
| H | LYS386 | |
| H | ARG463 | |
| I | LYS386 | |
| I | ARG463 | |
| J | LYS386 | |
| J | ARG463 | |
| K | LYS386 | |
| K | ARG463 | |
| L | LYS386 | |
| L | ARG463 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 36 |
| 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 | |
| A | ASP379 | |
| A | GLU461 | |
| B | LYS374 | |
| B | ASP379 | |
| B | GLU461 | |
| C | LYS374 | |
| C | ASP379 | |
| C | GLU461 | |
| D | LYS374 | |
| D | ASP379 | |
| D | GLU461 | |
| E | LYS374 | |
| E | ASP379 | |
| E | GLU461 | |
| F | LYS374 | |
| F | ASP379 | |
| F | GLU461 | |
| G | LYS374 | |
| G | ASP379 | |
| G | GLU461 | |
| H | LYS374 | |
| H | ASP379 | |
| H | GLU461 | |
| I | LYS374 | |
| I | ASP379 | |
| I | GLU461 | |
| J | LYS374 | |
| J | ASP379 | |
| J | GLU461 | |
| K | LYS374 | |
| K | ASP379 | |
| K | GLU461 | |
| L | LYS374 | |
| L | ASP379 | |
| L | GLU461 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| 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 | |
| G | LYS386 | |
| H | LYS386 | |
| I | LYS386 | |
| J | LYS386 | |
| K | LYS386 | |
| L | LYS386 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 36 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:35691342, ECO:0007744|PDB:7SRV |
| Chain | Residue | Details |
| A | ASP394 | |
| A | MET396 | |
| A | ASP399 | |
| B | ASP394 | |
| B | MET396 | |
| B | ASP399 | |
| C | ASP394 | |
| C | MET396 | |
| C | ASP399 | |
| D | ASP394 | |
| D | MET396 | |
| D | ASP399 | |
| E | ASP394 | |
| E | MET396 | |
| E | ASP399 | |
| F | ASP394 | |
| F | MET396 | |
| F | ASP399 | |
| G | ASP394 | |
| G | MET396 | |
| G | ASP399 | |
| H | ASP394 | |
| H | MET396 | |
| H | ASP399 | |
| I | ASP394 | |
| I | MET396 | |
| I | ASP399 | |
| J | ASP394 | |
| J | MET396 | |
| J | ASP399 | |
| K | ASP394 | |
| K | MET396 | |
| K | ASP399 | |
| L | ASP394 | |
| L | MET396 | |
| L | ASP399 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| 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 | |
| G | ASP459 | |
| H | ASP459 | |
| I | ASP459 | |
| J | ASP459 | |
| K | ASP459 | |
| L | ASP459 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| 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 | |
| G | LYS386 | |
| H | LYS386 | |
| I | LYS386 | |
| J | LYS386 | |
| K | LYS386 | |
| L | LYS386 |
