4R76
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 | 7 |
Details | BINDING SITE FOR RESIDUE ZN A 1001 |
Chain | Residue |
A | LYS374 |
A | ASP379 |
A | ASP399 |
A | GLU461 |
A | ZN1003 |
A | R5X1004 |
A | HOH1270 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CO3 A 1002 |
Chain | Residue |
A | GLY462 |
A | ARG463 |
A | LEU487 |
A | R5X1004 |
A | LYS374 |
A | ALA460 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN A 1003 |
Chain | Residue |
A | ASP379 |
A | ASP459 |
A | GLU461 |
A | ZN1001 |
A | R5X1004 |
site_id | AC4 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE R5X A 1004 |
Chain | Residue |
A | LYS374 |
A | ASP379 |
A | LYS386 |
A | MET392 |
A | ASP459 |
A | GLU461 |
A | LEU487 |
A | THR488 |
A | GLY489 |
A | LEU492 |
A | ALA577 |
A | ZN1001 |
A | CO31002 |
A | ZN1003 |
A | HOH1144 |
A | HOH1270 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 1005 |
Chain | Residue |
A | SER435 |
A | LYS436 |
B | SER435 |
B | LYS436 |
C | SER435 |
C | LYS436 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 A 1006 |
Chain | Residue |
A | TYR244 |
A | ASP249 |
A | TYR292 |
A | SER295 |
A | HOH1174 |
C | TYR541 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ZN B 1001 |
Chain | Residue |
B | LYS374 |
B | ASP379 |
B | ASP399 |
B | GLU461 |
B | ZN1003 |
B | R5X1004 |
B | HOH1225 |
site_id | AC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CO3 B 1002 |
Chain | Residue |
B | LYS374 |
B | ALA460 |
B | GLU461 |
B | GLY462 |
B | ARG463 |
B | LEU487 |
B | R5X1004 |
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 | R5X1004 |
site_id | BC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE R5X B 1004 |
Chain | Residue |
B | LYS374 |
B | ASP379 |
B | LYS386 |
B | PHE398 |
B | ASN457 |
B | ASP459 |
B | GLU461 |
B | LEU487 |
B | THR488 |
B | GLY489 |
B | ALA577 |
B | ZN1001 |
B | CO31002 |
B | ZN1003 |
B | HOH1134 |
B | HOH1225 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE 1PE B 1005 |
Chain | Residue |
B | TYR103 |
B | GLU316 |
B | LYS320 |
B | 1PE1006 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE 1PE B 1006 |
Chain | Residue |
B | TYR103 |
B | HIS108 |
B | PHE289 |
B | LYS320 |
B | TYR411 |
B | 1PE1005 |
site_id | BC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ZN C 1001 |
Chain | Residue |
C | LYS374 |
C | ASP379 |
C | ASP399 |
C | GLU461 |
C | ZN1003 |
C | R5X1004 |
C | HOH1255 |
site_id | BC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CO3 C 1002 |
Chain | Residue |
C | ALA460 |
C | GLY462 |
C | ARG463 |
C | LEU487 |
C | R5X1004 |
C | LYS374 |
site_id | BC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN C 1003 |
Chain | Residue |
C | ASP379 |
C | ASP459 |
C | GLU461 |
C | ZN1001 |
C | R5X1004 |
site_id | BC7 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE R5X C 1004 |
Chain | Residue |
C | LYS374 |
C | ASP379 |
C | LYS386 |
C | MET392 |
C | PHE398 |
C | ASN457 |
C | ASP459 |
C | GLU461 |
C | LEU487 |
C | THR488 |
C | GLY489 |
C | SER554 |
C | ALA577 |
C | ZN1001 |
C | CO31002 |
C | ZN1003 |
C | HOH1251 |
C | HOH1255 |
site_id | BC8 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ZN D 1001 |
Chain | Residue |
D | LYS374 |
D | ASP379 |
D | ASP399 |
D | GLU461 |
D | ZN1003 |
D | R5X1004 |
D | HOH1274 |
site_id | BC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CO3 D 1002 |
Chain | Residue |
D | LYS374 |
D | ALA460 |
D | GLY462 |
D | ARG463 |
D | LEU487 |
D | R5X1004 |
site_id | CC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN D 1003 |
Chain | Residue |
D | ASP379 |
D | ASP459 |
D | GLU461 |
D | ZN1001 |
D | R5X1004 |
site_id | CC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE R5X D 1004 |
Chain | Residue |
D | LYS374 |
D | ASP379 |
D | LYS386 |
D | ASN457 |
D | ASP459 |
D | GLU461 |
D | LEU487 |
D | THR488 |
D | GLY489 |
D | LEU492 |
D | SER554 |
D | ALA577 |
D | ZN1001 |
D | CO31002 |
D | ZN1003 |
D | HOH1274 |
site_id | CC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ZN E 1001 |
Chain | Residue |
E | LYS374 |
E | ASP379 |
E | ASP399 |
E | GLU461 |
E | ZN1003 |
E | R5X1004 |
E | HOH1157 |
site_id | CC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CO3 E 1002 |
Chain | Residue |
E | LYS374 |
E | ALA460 |
E | GLY462 |
E | ARG463 |
E | LEU487 |
E | R5X1004 |
site_id | CC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE ZN E 1003 |
Chain | Residue |
E | ASP379 |
E | LYS386 |
E | ASP459 |
E | GLU461 |
E | ZN1001 |
E | R5X1004 |
site_id | CC6 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE R5X E 1004 |
Chain | Residue |
E | LYS374 |
E | ASP379 |
E | LYS386 |
E | PHE398 |
E | ASN457 |
E | ASP459 |
E | GLU461 |
E | LEU487 |
E | THR488 |
E | GLY489 |
E | ZN1001 |
E | CO31002 |
E | ZN1003 |
E | HOH1141 |
E | HOH1157 |
site_id | CC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 E 1005 |
Chain | Residue |
D | SER435 |
D | LYS436 |
E | SER435 |
E | LYS436 |
F | SER435 |
F | LYS436 |
site_id | CC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE 1PE E 1006 |
Chain | Residue |
E | TYR103 |
E | HIS108 |
E | LEU321 |
E | TYR411 |
site_id | CC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE 1PE E 1007 |
Chain | Residue |
E | ASN511 |
site_id | DC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ZN F 1001 |
Chain | Residue |
F | LYS374 |
F | ASP379 |
F | ASP399 |
F | GLU461 |
F | ZN1003 |
F | R5X1004 |
F | HOH1219 |
site_id | DC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 E 1008 |
Chain | Residue |
E | GLU102 |
E | TYR103 |
E | ASN104 |
E | HOH1178 |
site_id | DC3 |
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 | R5X1004 |
site_id | DC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN F 1003 |
Chain | Residue |
F | ASP379 |
F | ASP459 |
F | GLU461 |
F | ZN1001 |
F | R5X1004 |
site_id | DC5 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE R5X F 1004 |
Chain | Residue |
F | LYS374 |
F | ASP379 |
F | LYS386 |
F | MET392 |
F | PHE398 |
F | ASN457 |
F | ASP459 |
F | GLU461 |
F | LEU487 |
F | THR488 |
F | GLY489 |
F | LEU492 |
F | ALA577 |
F | ZN1001 |
F | CO31002 |
F | ZN1003 |
F | HOH1219 |
site_id | DC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE 1PE F 1005 |
Chain | Residue |
F | TYR103 |
F | LYS320 |
F | SO41008 |
site_id | DC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE 1PE F 1006 |
Chain | Residue |
F | TYR103 |
F | ASN104 |
F | HIS108 |
F | LYS320 |
F | TYR411 |
F | HOH1142 |
site_id | DC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE 1PE F 1007 |
Chain | Residue |
F | SER93 |
F | LEU94 |
F | ASP95 |
site_id | DC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 F 1008 |
Chain | Residue |
F | ILE101 |
F | TYR103 |
F | ASN104 |
F | 1PE1005 |
F | HOH1172 |
site_id | EC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ZN G 1001 |
Chain | Residue |
G | LYS374 |
G | ASP379 |
G | ASP399 |
G | GLU461 |
G | ZN1003 |
G | R5X1004 |
G | HOH1148 |
site_id | EC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CO3 G 1002 |
Chain | Residue |
G | LYS374 |
G | ALA460 |
G | GLY462 |
G | ARG463 |
G | LEU487 |
G | R5X1004 |
site_id | EC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN G 1003 |
Chain | Residue |
G | ASP379 |
G | ASP459 |
G | GLU461 |
G | ZN1001 |
G | R5X1004 |
site_id | EC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE R5X G 1004 |
Chain | Residue |
G | LYS374 |
G | ASP379 |
G | LYS386 |
G | MET396 |
G | ASN457 |
G | ASP459 |
G | GLU461 |
G | LEU487 |
G | THR488 |
G | GLY489 |
G | LEU492 |
G | SER554 |
G | ALA577 |
G | ZN1001 |
G | CO31002 |
G | ZN1003 |
G | HOH1148 |
site_id | EC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE 1PE G 1005 |
Chain | Residue |
G | TYR103 |
G | HIS108 |
G | PHE289 |
G | LYS320 |
G | TYR411 |
site_id | EC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE 1PE G 1006 |
Chain | Residue |
G | TYR103 |
G | GLU316 |
G | GLN319 |
G | LYS320 |
G | HOH1244 |
site_id | EC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ZN H 1001 |
Chain | Residue |
H | LYS374 |
H | ASP379 |
H | ASP399 |
H | GLU461 |
H | ZN1003 |
H | R5X1004 |
H | HOH1233 |
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 | R5X1004 |
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 | R5X1004 |
site_id | FC1 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE R5X H 1004 |
Chain | Residue |
H | LYS374 |
H | ASP379 |
H | LYS386 |
H | ASN457 |
H | ASP459 |
H | GLU461 |
H | LEU487 |
H | THR488 |
H | GLY489 |
H | ALA577 |
H | ZN1001 |
H | CO31002 |
H | ZN1003 |
H | HOH1136 |
H | HOH1233 |
site_id | FC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 H 1005 |
Chain | Residue |
G | SER435 |
G | LYS436 |
H | SER435 |
H | LYS436 |
I | SER435 |
I | LYS436 |
site_id | FC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE 1PE H 1006 |
Chain | Residue |
H | TYR103 |
H | ASN104 |
H | HIS108 |
H | LYS320 |
H | TYR411 |
site_id | FC4 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ZN I 1001 |
Chain | Residue |
I | LYS374 |
I | ASP379 |
I | ASP399 |
I | GLU461 |
I | ZN1003 |
I | R5X1004 |
I | HOH1242 |
site_id | FC5 |
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 | R5X1004 |
site_id | FC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN I 1003 |
Chain | Residue |
I | ASP379 |
I | ASP459 |
I | GLU461 |
I | ZN1001 |
I | R5X1004 |
site_id | FC7 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE R5X I 1004 |
Chain | Residue |
I | LYS374 |
I | ASP379 |
I | LYS386 |
I | MET392 |
I | PHE398 |
I | ASP459 |
I | GLU461 |
I | ARG463 |
I | LEU487 |
I | THR488 |
I | GLY489 |
I | ALA577 |
I | ZN1001 |
I | CO31002 |
I | ZN1003 |
I | HOH1242 |
site_id | FC8 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE 1PE I 1005 |
Chain | Residue |
I | TYR103 |
I | GLU316 |
I | LYS320 |
site_id | FC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE 1PE I 1006 |
Chain | Residue |
I | TYR103 |
I | ASN104 |
I | PHE289 |
I | LYS320 |
I | TYR411 |
site_id | GC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ZN J 1001 |
Chain | Residue |
J | LYS374 |
J | ASP379 |
J | ASP399 |
J | GLU461 |
J | ZN1003 |
J | R5X1004 |
J | HOH1271 |
site_id | GC2 |
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 | R5X1004 |
site_id | GC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN J 1003 |
Chain | Residue |
J | ASP379 |
J | ASP459 |
J | GLU461 |
J | ZN1001 |
J | R5X1004 |
site_id | GC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE R5X J 1004 |
Chain | Residue |
J | LYS374 |
J | ASP379 |
J | LYS386 |
J | MET392 |
J | ASP459 |
J | GLU461 |
J | LEU487 |
J | THR488 |
J | GLY489 |
J | ALA577 |
J | ZN1001 |
J | CO31002 |
J | ZN1003 |
site_id | GC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE 1PE J 1005 |
Chain | Residue |
J | TYR103 |
J | HIS108 |
J | PHE289 |
J | TYR411 |
site_id | GC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ZN K 1001 |
Chain | Residue |
K | LYS374 |
K | ASP379 |
K | ASP399 |
K | GLU461 |
K | ZN1003 |
K | R5X1004 |
K | HOH1255 |
site_id | GC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CO3 K 1002 |
Chain | Residue |
K | LYS374 |
K | ALA460 |
K | GLY462 |
K | ARG463 |
K | LEU487 |
K | R5X1004 |
site_id | GC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN K 1003 |
Chain | Residue |
K | ASP379 |
K | ASP459 |
K | GLU461 |
K | ZN1001 |
K | R5X1004 |
site_id | GC9 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE R5X K 1004 |
Chain | Residue |
K | LYS374 |
K | ASP379 |
K | LYS386 |
K | MET392 |
K | PHE398 |
K | ASP459 |
K | GLU461 |
K | LEU487 |
K | THR488 |
K | GLY489 |
K | LEU492 |
K | SER554 |
K | ZN1001 |
K | CO31002 |
K | ZN1003 |
K | HOH1181 |
K | HOH1255 |
K | HOH1262 |
site_id | HC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SO4 K 1005 |
Chain | Residue |
J | SER435 |
J | LYS436 |
K | SER435 |
K | LYS436 |
L | SER435 |
L | LYS436 |
site_id | HC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE 1PE K 1006 |
Chain | Residue |
K | TYR103 |
K | HIS108 |
K | PHE289 |
K | TYR411 |
site_id | HC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE ZN L 1001 |
Chain | Residue |
L | LYS374 |
L | ASP379 |
L | ASP399 |
L | GLU461 |
L | ZN1003 |
L | R5X1004 |
L | HOH1240 |
site_id | HC4 |
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 | R5X1004 |
site_id | HC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ZN L 1003 |
Chain | Residue |
L | ASP379 |
L | ASP459 |
L | GLU461 |
L | ZN1001 |
L | R5X1004 |
site_id | HC6 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE R5X L 1004 |
Chain | Residue |
L | LYS374 |
L | ASP379 |
L | LYS386 |
L | PHE398 |
L | ASN457 |
L | ASP459 |
L | GLU461 |
L | LEU487 |
L | THR488 |
L | GLY489 |
L | SER554 |
L | ALA577 |
L | ZN1001 |
L | CO31002 |
L | ZN1003 |
L | HOH1240 |
site_id | HC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE 1PE L 1005 |
Chain | Residue |
L | TYR103 |
L | ASN104 |
L | HIS108 |
L | TYR411 |
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 |