4X2T
X-ray crystal structure of the orally available aminopeptidase inhibitor, Tosedostat, bound to the M17 Leucyl Aminopeptidase from P. falciparum
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 | 5 |
| Details | binding site for residue ZN A 701 |
| Chain | Residue |
| A | ASP379 |
| A | ASP459 |
| A | GLU461 |
| A | ZN702 |
| A | TOD703 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue ZN A 702 |
| Chain | Residue |
| A | ZN701 |
| A | TOD703 |
| A | LYS374 |
| A | ASP379 |
| A | ASP399 |
| A | GLU461 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue TOD A 703 |
| Chain | Residue |
| A | LYS374 |
| A | ASP379 |
| A | LYS386 |
| A | ASP459 |
| A | ALA460 |
| A | GLU461 |
| A | LEU487 |
| A | GLY489 |
| A | ZN701 |
| A | ZN702 |
| A | CO3704 |
| A | HOH829 |
| A | HOH830 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue CO3 A 704 |
| Chain | Residue |
| A | ALA460 |
| A | GLY462 |
| A | ARG463 |
| A | LEU487 |
| A | TOD703 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 706 |
| Chain | Residue |
| A | ASP249 |
| A | TYR292 |
| A | SER295 |
| A | LYS587 |
| A | PRO588 |
| C | TYR541 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 707 |
| Chain | Residue |
| A | ILE529 |
| A | ILE530 |
| A | ASN531 |
| F | TYR499 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue 1PE A 708 |
| Chain | Residue |
| A | TYR103 |
| A | ASN104 |
| A | HIS108 |
| A | LYS320 |
| A | TYR411 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue CO3 B 1001 |
| Chain | Residue |
| B | LYS374 |
| B | ALA460 |
| B | GLU461 |
| B | GLY462 |
| B | ARG463 |
| B | LEU487 |
| B | TOD1004 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 1002 |
| Chain | Residue |
| B | ASP379 |
| B | ASP459 |
| B | GLU461 |
| B | ZN1003 |
| B | TOD1004 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue ZN B 1003 |
| Chain | Residue |
| B | LYS374 |
| B | ASP379 |
| B | ASP399 |
| B | GLU461 |
| B | ZN1002 |
| B | TOD1004 |
| site_id | AD2 |
| Number of Residues | 11 |
| Details | binding site for residue TOD B 1004 |
| Chain | Residue |
| B | LYS374 |
| B | ASP379 |
| B | LYS386 |
| B | ASP459 |
| B | GLU461 |
| B | LEU487 |
| B | GLY489 |
| B | ALA490 |
| B | CO31001 |
| B | ZN1002 |
| B | ZN1003 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 B 1005 |
| Chain | Residue |
| A | SER435 |
| A | LYS436 |
| B | SER435 |
| B | LYS436 |
| C | SER435 |
| C | LYS436 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue 1PE B 1006 |
| Chain | Residue |
| B | TYR103 |
| B | HIS108 |
| B | LYS320 |
| B | TYR411 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue ZN C 701 |
| Chain | Residue |
| C | LYS374 |
| C | ASP379 |
| C | ASP399 |
| C | GLU461 |
| C | ZN702 |
| C | TOD703 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue ZN C 702 |
| Chain | Residue |
| C | ASP379 |
| C | ASP459 |
| C | GLU461 |
| C | ZN701 |
| C | TOD703 |
| site_id | AD7 |
| Number of Residues | 11 |
| Details | binding site for residue TOD C 703 |
| Chain | Residue |
| C | GLU461 |
| C | LEU487 |
| C | GLY489 |
| C | ZN701 |
| C | ZN702 |
| C | CO3704 |
| C | LYS374 |
| C | ASP379 |
| C | LYS386 |
| C | ASN457 |
| C | ASP459 |
| site_id | AD8 |
| Number of Residues | 7 |
| Details | binding site for residue CO3 C 704 |
| Chain | Residue |
| C | LYS374 |
| C | ALA460 |
| C | GLU461 |
| C | GLY462 |
| C | ARG463 |
| C | LEU487 |
| C | TOD703 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 C 705 |
| Chain | Residue |
| C | GLY126 |
| C | LEU219 |
| C | SER220 |
| site_id | AE1 |
| Number of Residues | 6 |
| Details | binding site for residue 1PE C 706 |
| Chain | Residue |
| C | TYR103 |
| C | GLU316 |
| C | GLN319 |
| C | LYS320 |
| C | 1PE707 |
| C | HOH852 |
| site_id | AE2 |
| Number of Residues | 6 |
| Details | binding site for residue 1PE C 707 |
| Chain | Residue |
| C | TYR103 |
| C | ASN104 |
| C | HIS108 |
| C | LYS320 |
| C | TYR411 |
| C | 1PE706 |
| site_id | AE3 |
| Number of Residues | 4 |
| Details | binding site for residue ZN D 701 |
| Chain | Residue |
| D | ASP379 |
| D | ASP459 |
| D | GLU461 |
| D | ZN702 |
| site_id | AE4 |
| Number of Residues | 5 |
| Details | binding site for residue ZN D 702 |
| Chain | Residue |
| D | LYS374 |
| D | ASP379 |
| D | ASP399 |
| D | GLU461 |
| D | ZN701 |
| site_id | AE5 |
| Number of Residues | 6 |
| Details | binding site for residue CO3 D 703 |
| Chain | Residue |
| D | LYS374 |
| D | ALA460 |
| D | GLU461 |
| D | GLY462 |
| D | ARG463 |
| D | LEU487 |
| site_id | AE6 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 D 704 |
| Chain | Residue |
| A | PHE156 |
| A | ASN161 |
| D | TYR176 |
| D | MET177 |
| D | PHE178 |
| D | SER184 |
| site_id | AE7 |
| Number of Residues | 6 |
| Details | binding site for residue 1PE D 705 |
| Chain | Residue |
| D | TYR103 |
| D | ASN104 |
| D | HIS108 |
| D | LYS320 |
| D | TYR411 |
| D | 1PE706 |
| site_id | AE8 |
| Number of Residues | 4 |
| Details | binding site for residue 1PE D 706 |
| Chain | Residue |
| D | TYR103 |
| D | GLU316 |
| D | LYS320 |
| D | 1PE705 |
| site_id | AE9 |
| Number of Residues | 6 |
| Details | binding site for residue ZN E 701 |
| Chain | Residue |
| E | LYS374 |
| E | ASP379 |
| E | ASP399 |
| E | GLU461 |
| E | ZN702 |
| E | TOD703 |
| site_id | AF1 |
| Number of Residues | 5 |
| Details | binding site for residue ZN E 702 |
| Chain | Residue |
| E | ASP379 |
| E | ASP459 |
| E | GLU461 |
| E | ZN701 |
| E | TOD703 |
| site_id | AF2 |
| Number of Residues | 12 |
| Details | binding site for residue TOD E 703 |
| Chain | Residue |
| E | LYS374 |
| E | ASP379 |
| E | LYS386 |
| E | ASP399 |
| E | ASP459 |
| E | GLU461 |
| E | LEU487 |
| E | THR488 |
| E | GLY489 |
| E | ZN701 |
| E | ZN702 |
| E | CO3704 |
| site_id | AF3 |
| Number of Residues | 6 |
| Details | binding site for residue CO3 E 704 |
| Chain | Residue |
| E | LYS374 |
| E | ALA460 |
| E | GLY462 |
| E | ARG463 |
| E | LEU487 |
| E | TOD703 |
| site_id | AF4 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 E 705 |
| Chain | Residue |
| D | SER435 |
| D | LYS436 |
| E | SER435 |
| E | LYS436 |
| F | SER435 |
| F | LYS436 |
| site_id | AF5 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 E 706 |
| Chain | Residue |
| C | PHE156 |
| E | TYR176 |
| E | PHE178 |
| E | SER184 |
| site_id | AF6 |
| Number of Residues | 5 |
| Details | binding site for residue 1PE E 707 |
| Chain | Residue |
| E | TYR103 |
| E | HIS108 |
| E | PHE289 |
| E | LEU321 |
| E | TYR411 |
| site_id | AF7 |
| Number of Residues | 6 |
| Details | binding site for residue ZN F 701 |
| Chain | Residue |
| F | ASP379 |
| F | LYS386 |
| F | ASP459 |
| F | GLU461 |
| F | ZN702 |
| F | TOD703 |
| site_id | AF8 |
| Number of Residues | 6 |
| Details | binding site for residue ZN F 702 |
| Chain | Residue |
| F | LYS374 |
| F | ASP379 |
| F | ASP399 |
| F | GLU461 |
| F | ZN701 |
| F | TOD703 |
| site_id | AF9 |
| Number of Residues | 13 |
| Details | binding site for residue TOD F 703 |
| Chain | Residue |
| F | LYS374 |
| F | ASP379 |
| F | LYS386 |
| F | ASP459 |
| F | GLU461 |
| F | LEU487 |
| F | GLY489 |
| F | ALA490 |
| F | TYR493 |
| F | ZN701 |
| F | ZN702 |
| F | CO3704 |
| F | HOH850 |
| site_id | AG1 |
| Number of Residues | 6 |
| Details | binding site for residue CO3 F 704 |
| Chain | Residue |
| F | ALA460 |
| F | GLU461 |
| F | GLY462 |
| F | ARG463 |
| F | LEU487 |
| F | TOD703 |
| site_id | AG2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN G 701 |
| Chain | Residue |
| G | ASP379 |
| G | ASP459 |
| G | GLU461 |
| G | ZN702 |
| G | TOD703 |
| site_id | AG3 |
| Number of Residues | 8 |
| Details | binding site for residue ZN G 702 |
| Chain | Residue |
| G | LYS374 |
| G | ASP379 |
| G | ASP399 |
| G | GLU461 |
| G | ZN701 |
| G | TOD703 |
| G | CO3704 |
| G | HOH847 |
| site_id | AG4 |
| Number of Residues | 13 |
| Details | binding site for residue TOD G 703 |
| Chain | Residue |
| G | LYS374 |
| G | ASP379 |
| G | LYS386 |
| G | ASP459 |
| G | GLU461 |
| G | LEU487 |
| G | GLY489 |
| G | ILE547 |
| G | ZN701 |
| G | ZN702 |
| G | CO3704 |
| G | HOH847 |
| G | HOH883 |
| site_id | AG5 |
| Number of Residues | 7 |
| Details | binding site for residue CO3 G 704 |
| Chain | Residue |
| G | ALA460 |
| G | GLU461 |
| G | GLY462 |
| G | ARG463 |
| G | LEU487 |
| G | ZN702 |
| G | TOD703 |
| site_id | AG6 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 G 705 |
| Chain | Residue |
| G | HOH818 |
| G | HOH893 |
| site_id | AG7 |
| Number of Residues | 5 |
| Details | binding site for residue SO4 G 706 |
| Chain | Residue |
| A | LYS111 |
| G | GLY126 |
| G | SER220 |
| G | HOH891 |
| J | LYS164 |
| site_id | AG8 |
| Number of Residues | 3 |
| Details | binding site for residue 1PE G 707 |
| Chain | Residue |
| G | ASN104 |
| G | HIS108 |
| G | LYS320 |
| site_id | AG9 |
| Number of Residues | 4 |
| Details | binding site for residue 1PE G 708 |
| Chain | Residue |
| G | TYR103 |
| G | GLU316 |
| G | GLN319 |
| G | LYS320 |
| site_id | AH1 |
| Number of Residues | 7 |
| Details | binding site for residue ZN H 701 |
| Chain | Residue |
| H | LYS374 |
| H | ASP379 |
| H | ASP399 |
| H | GLU461 |
| H | ZN702 |
| H | TOD703 |
| H | HOH840 |
| site_id | AH2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN H 702 |
| Chain | Residue |
| H | ASP379 |
| H | ASP459 |
| H | GLU461 |
| H | ZN701 |
| H | TOD703 |
| site_id | AH3 |
| Number of Residues | 12 |
| Details | binding site for residue TOD H 703 |
| Chain | Residue |
| H | LYS374 |
| H | ASP379 |
| H | LYS386 |
| H | ASP459 |
| H | ALA460 |
| H | GLU461 |
| H | LEU487 |
| H | GLY489 |
| H | ZN701 |
| H | ZN702 |
| H | CO3704 |
| H | HOH840 |
| site_id | AH4 |
| Number of Residues | 8 |
| Details | binding site for residue CO3 H 704 |
| Chain | Residue |
| H | LYS374 |
| H | ASP459 |
| H | ALA460 |
| H | GLU461 |
| H | GLY462 |
| H | ARG463 |
| H | LEU487 |
| H | TOD703 |
| site_id | AH5 |
| Number of Residues | 7 |
| Details | binding site for residue 1PE H 705 |
| Chain | Residue |
| H | TYR103 |
| H | ASN104 |
| H | HIS108 |
| H | PHE289 |
| H | LYS320 |
| H | LEU321 |
| H | TYR411 |
| site_id | AH6 |
| Number of Residues | 5 |
| Details | binding site for residue ZN I 701 |
| Chain | Residue |
| I | ASP379 |
| I | ASP459 |
| I | GLU461 |
| I | ZN702 |
| I | TOD703 |
| site_id | AH7 |
| Number of Residues | 8 |
| Details | binding site for residue ZN I 702 |
| Chain | Residue |
| I | LYS374 |
| I | ASP379 |
| I | ASP399 |
| I | GLU461 |
| I | ZN701 |
| I | TOD703 |
| I | CO3704 |
| I | HOH833 |
| site_id | AH8 |
| Number of Residues | 13 |
| Details | binding site for residue TOD I 703 |
| Chain | Residue |
| I | LYS374 |
| I | ASP379 |
| I | LYS386 |
| I | ASP459 |
| I | GLU461 |
| I | ARG463 |
| I | LEU487 |
| I | GLY489 |
| I | SER554 |
| I | ZN701 |
| I | ZN702 |
| I | CO3704 |
| I | HOH884 |
| site_id | AH9 |
| Number of Residues | 8 |
| Details | binding site for residue CO3 I 704 |
| Chain | Residue |
| I | ASP459 |
| I | ALA460 |
| I | GLU461 |
| I | GLY462 |
| I | ARG463 |
| I | LEU487 |
| I | ZN702 |
| I | TOD703 |
| site_id | AI1 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 I 705 |
| Chain | Residue |
| G | SER435 |
| G | LYS436 |
| H | SER435 |
| H | LYS436 |
| I | SER435 |
| I | LYS436 |
| site_id | AI2 |
| Number of Residues | 5 |
| Details | binding site for residue ZN J 701 |
| Chain | Residue |
| J | ASP379 |
| J | ASP459 |
| J | GLU461 |
| J | ZN702 |
| J | TOD703 |
| site_id | AI3 |
| Number of Residues | 6 |
| Details | binding site for residue ZN J 702 |
| Chain | Residue |
| J | LYS374 |
| J | ASP379 |
| J | ASP399 |
| J | GLU461 |
| J | ZN701 |
| J | TOD703 |
| site_id | AI4 |
| Number of Residues | 11 |
| Details | binding site for residue TOD J 703 |
| Chain | Residue |
| J | LYS374 |
| J | ASP379 |
| J | LYS386 |
| J | ASP459 |
| J | GLU461 |
| J | LEU487 |
| J | THR488 |
| J | GLY489 |
| J | ZN701 |
| J | ZN702 |
| J | CO3704 |
| site_id | AI5 |
| Number of Residues | 7 |
| Details | binding site for residue CO3 J 704 |
| Chain | Residue |
| J | LYS374 |
| J | ALA460 |
| J | GLU461 |
| J | GLY462 |
| J | ARG463 |
| J | LEU487 |
| J | TOD703 |
| site_id | AI6 |
| Number of Residues | 5 |
| Details | binding site for residue ZN K 701 |
| Chain | Residue |
| K | ASP379 |
| K | ASP459 |
| K | GLU461 |
| K | ZN702 |
| K | TOD703 |
| site_id | AI7 |
| Number of Residues | 6 |
| Details | binding site for residue ZN K 702 |
| Chain | Residue |
| K | LYS374 |
| K | ASP379 |
| K | ASP399 |
| K | GLU461 |
| K | ZN701 |
| K | TOD703 |
| site_id | AI8 |
| Number of Residues | 13 |
| Details | binding site for residue TOD K 703 |
| Chain | Residue |
| K | LYS374 |
| K | ASP379 |
| K | LYS386 |
| K | ASP459 |
| K | ALA460 |
| K | GLU461 |
| K | LEU487 |
| K | THR488 |
| K | GLY489 |
| K | TYR493 |
| K | ZN701 |
| K | ZN702 |
| K | CO3704 |
| site_id | AI9 |
| Number of Residues | 6 |
| Details | binding site for residue CO3 K 704 |
| Chain | Residue |
| K | ALA460 |
| K | GLU461 |
| K | GLY462 |
| K | ARG463 |
| K | LEU487 |
| K | TOD703 |
| site_id | AJ1 |
| Number of Residues | 5 |
| Details | binding site for residue ZN L 701 |
| Chain | Residue |
| L | ASP379 |
| L | ASP459 |
| L | GLU461 |
| L | ZN702 |
| L | TOD703 |
| site_id | AJ2 |
| Number of Residues | 6 |
| Details | binding site for residue ZN L 702 |
| Chain | Residue |
| L | LYS374 |
| L | ASP379 |
| L | ASP399 |
| L | GLU461 |
| L | ZN701 |
| L | TOD703 |
| site_id | AJ3 |
| Number of Residues | 11 |
| Details | binding site for residue TOD L 703 |
| Chain | Residue |
| L | LYS374 |
| L | ASP379 |
| L | LYS386 |
| L | ASP459 |
| L | GLU461 |
| L | LEU487 |
| L | THR488 |
| L | GLY489 |
| L | ZN701 |
| L | ZN702 |
| L | CO3704 |
| site_id | AJ4 |
| Number of Residues | 7 |
| Details | binding site for residue CO3 L 704 |
| Chain | Residue |
| L | LYS374 |
| L | ALA460 |
| L | GLU461 |
| L | GLY462 |
| L | ARG463 |
| L | LEU487 |
| L | TOD703 |
| site_id | AJ5 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 L 705 |
| Chain | Residue |
| J | SER435 |
| J | LYS436 |
| K | SER435 |
| K | LYS436 |
| L | SER435 |
| L | LYS436 |
| site_id | AJ6 |
| Number of Residues | 10 |
| Details | binding site for Di-peptide LYS G 512 and ASP G 603 |
| Chain | Residue |
| G | GLU508 |
| G | LEU509 |
| G | ILE510 |
| G | ASN511 |
| G | ILE513 |
| G | LEU514 |
| G | GLN515 |
| G | SER516 |
| G | LEU601 |
| G | ASN602 |
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 | |
| E | ARG463 | |
| F | LYS386 | |
| F | ARG463 | |
| G | LYS386 | |
| G | ARG463 | |
| H | LYS386 | |
| H | ARG463 | |
| I | LYS386 | |
| I | ARG463 | |
| J | LYS386 | |
| A | ARG463 | |
| J | ARG463 | |
| K | LYS386 | |
| K | ARG463 | |
| L | LYS386 | |
| L | ARG463 | |
| B | LYS386 | |
| B | ARG463 | |
| C | LYS386 | |
| C | ARG463 | |
| D | LYS386 | |
| D | ARG463 | |
| E | LYS386 |
| 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 | |
| D | LYS374 | |
| D | ASP379 | |
| D | GLU461 | |
| E | LYS374 | |
| E | ASP379 | |
| E | GLU461 | |
| F | LYS374 | |
| F | ASP379 | |
| F | GLU461 | |
| G | LYS374 | |
| A | ASP379 | |
| G | ASP379 | |
| G | GLU461 | |
| H | LYS374 | |
| H | ASP379 | |
| H | GLU461 | |
| I | LYS374 | |
| I | ASP379 | |
| I | GLU461 | |
| J | LYS374 | |
| J | ASP379 | |
| A | GLU461 | |
| J | GLU461 | |
| K | LYS374 | |
| K | ASP379 | |
| K | GLU461 | |
| L | LYS374 | |
| L | ASP379 | |
| L | GLU461 | |
| B | LYS374 | |
| B | ASP379 | |
| B | GLU461 | |
| C | LYS374 | |
| C | ASP379 | |
| C | 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 | |
| J | LYS386 | |
| K | LYS386 | |
| L | LYS386 | |
| B | LYS386 | |
| C | LYS386 | |
| D | LYS386 | |
| E | LYS386 | |
| F | LYS386 | |
| G | LYS386 | |
| H | LYS386 | |
| I | 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 | |
| D | ASP394 | |
| D | MET396 | |
| D | ASP399 | |
| E | ASP394 | |
| E | MET396 | |
| E | ASP399 | |
| F | ASP394 | |
| F | MET396 | |
| F | ASP399 | |
| G | ASP394 | |
| A | MET396 | |
| G | MET396 | |
| G | ASP399 | |
| H | ASP394 | |
| H | MET396 | |
| H | ASP399 | |
| I | ASP394 | |
| I | MET396 | |
| I | ASP399 | |
| J | ASP394 | |
| J | MET396 | |
| A | ASP399 | |
| J | ASP399 | |
| K | ASP394 | |
| K | MET396 | |
| K | ASP399 | |
| L | ASP394 | |
| L | MET396 | |
| L | ASP399 | |
| B | ASP394 | |
| B | MET396 | |
| B | ASP399 | |
| C | ASP394 | |
| C | MET396 | |
| C | 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 | |
| J | ASP459 | |
| K | ASP459 | |
| L | ASP459 | |
| B | ASP459 | |
| C | ASP459 | |
| D | ASP459 | |
| E | ASP459 | |
| F | ASP459 | |
| G | ASP459 | |
| H | ASP459 | |
| I | 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 | |
| J | LYS386 | |
| K | LYS386 | |
| L | LYS386 | |
| B | LYS386 | |
| C | LYS386 | |
| D | LYS386 | |
| E | LYS386 | |
| F | LYS386 | |
| G | LYS386 | |
| H | LYS386 | |
| I | LYS386 |
