3H8G
Bestatin complex structure of leucine aminopeptidase from Pseudomonas putida
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004177 | molecular_function | aminopeptidase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006508 | biological_process | proteolysis |
| A | 0008235 | molecular_function | metalloexopeptidase activity |
| 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 | 0004177 | molecular_function | aminopeptidase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006508 | biological_process | proteolysis |
| B | 0008235 | molecular_function | metalloexopeptidase activity |
| 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 | 0004177 | molecular_function | aminopeptidase activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006508 | biological_process | proteolysis |
| C | 0008235 | molecular_function | metalloexopeptidase activity |
| 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 | 0004177 | molecular_function | aminopeptidase activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0006508 | biological_process | proteolysis |
| D | 0008235 | molecular_function | metalloexopeptidase activity |
| 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 | 0004177 | molecular_function | aminopeptidase activity |
| E | 0005737 | cellular_component | cytoplasm |
| E | 0006508 | biological_process | proteolysis |
| E | 0008235 | molecular_function | metalloexopeptidase activity |
| 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 | 0004177 | molecular_function | aminopeptidase activity |
| F | 0005737 | cellular_component | cytoplasm |
| F | 0006508 | biological_process | proteolysis |
| F | 0008235 | molecular_function | metalloexopeptidase activity |
| 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 PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN A 501 |
| Chain | Residue |
| A | LYS267 |
| A | ASP272 |
| A | ASP290 |
| A | GLU351 |
| A | MN502 |
| A | BCT504 |
| A | BES505 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN A 502 |
| Chain | Residue |
| A | GLU351 |
| A | ZN501 |
| A | BES505 |
| A | ASP272 |
| A | ASP349 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K A 503 |
| Chain | Residue |
| A | LEU189 |
| A | GLY190 |
| A | LEU192 |
| A | LYS288 |
| A | MET291 |
| A | HOH514 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BCT A 504 |
| Chain | Residue |
| A | LYS267 |
| A | ALA350 |
| A | GLU351 |
| A | GLY352 |
| A | ARG353 |
| A | LEU377 |
| A | ZN501 |
| A | BES505 |
| site_id | AC5 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE BES A 505 |
| Chain | Residue |
| A | LYS267 |
| A | ASP272 |
| A | LYS279 |
| A | MET287 |
| A | ASP290 |
| A | ASP349 |
| A | GLU351 |
| A | THR376 |
| A | LEU377 |
| A | THR378 |
| A | GLY379 |
| A | ILE437 |
| A | ALA466 |
| A | TRP470 |
| A | ZN501 |
| A | MN502 |
| A | BCT504 |
| A | HOH2935 |
| A | HOH2940 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN B 501 |
| Chain | Residue |
| B | LYS267 |
| B | ASP272 |
| B | ASP290 |
| B | GLU351 |
| B | MN502 |
| B | BCT504 |
| B | BES505 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN B 502 |
| Chain | Residue |
| B | ASP272 |
| B | ASP349 |
| B | GLU351 |
| B | ZN501 |
| B | BES505 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 503 |
| Chain | Residue |
| B | LEU189 |
| B | GLY190 |
| B | LEU192 |
| B | LYS288 |
| B | MET291 |
| B | HOH524 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BCT B 504 |
| Chain | Residue |
| B | LYS267 |
| B | ALA350 |
| B | GLU351 |
| B | GLY352 |
| B | ARG353 |
| B | LEU377 |
| B | ZN501 |
| B | BES505 |
| site_id | BC1 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE BES B 505 |
| Chain | Residue |
| B | LYS267 |
| B | ASP272 |
| B | LYS279 |
| B | MET287 |
| B | ASP290 |
| B | ASP349 |
| B | GLU351 |
| B | THR376 |
| B | LEU377 |
| B | THR378 |
| B | GLY379 |
| B | ALA466 |
| B | TRP470 |
| B | ZN501 |
| B | MN502 |
| B | BCT504 |
| B | HOH2809 |
| B | HOH3487 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN C 501 |
| Chain | Residue |
| C | LYS267 |
| C | ASP272 |
| C | ASP290 |
| C | GLU351 |
| C | MN502 |
| C | BCT504 |
| C | BES505 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN C 502 |
| Chain | Residue |
| C | ZN501 |
| C | BES505 |
| C | ASP272 |
| C | ASP349 |
| C | GLU351 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K C 503 |
| Chain | Residue |
| C | LEU189 |
| C | GLY190 |
| C | LEU192 |
| C | LYS288 |
| C | MET291 |
| C | HOH518 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BCT C 504 |
| Chain | Residue |
| C | LYS267 |
| C | ALA350 |
| C | GLU351 |
| C | GLY352 |
| C | ARG353 |
| C | LEU377 |
| C | ZN501 |
| C | BES505 |
| site_id | BC6 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE BES C 505 |
| Chain | Residue |
| C | LYS267 |
| C | ASP272 |
| C | LYS279 |
| C | MET287 |
| C | ASP290 |
| C | ASP349 |
| C | GLU351 |
| C | THR376 |
| C | LEU377 |
| C | THR378 |
| C | GLY379 |
| C | ALA466 |
| C | TRP470 |
| C | ZN501 |
| C | MN502 |
| C | BCT504 |
| C | HOH2928 |
| C | HOH3103 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN D 501 |
| Chain | Residue |
| D | LYS267 |
| D | ASP272 |
| D | ASP290 |
| D | GLU351 |
| D | MN502 |
| D | BCT504 |
| D | BES505 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN D 502 |
| Chain | Residue |
| D | ASP272 |
| D | ASP349 |
| D | GLU351 |
| D | ZN501 |
| D | BES505 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K D 503 |
| Chain | Residue |
| D | LEU189 |
| D | GLY190 |
| D | LEU192 |
| D | LYS288 |
| D | MET291 |
| D | HOH526 |
| site_id | CC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BCT D 504 |
| Chain | Residue |
| D | LYS267 |
| D | ALA350 |
| D | GLU351 |
| D | GLY352 |
| D | ARG353 |
| D | LEU377 |
| D | ZN501 |
| D | BES505 |
| site_id | CC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE BES D 505 |
| Chain | Residue |
| D | LYS267 |
| D | ASP272 |
| D | LYS279 |
| D | MET287 |
| D | ASP290 |
| D | ASP349 |
| D | GLU351 |
| D | THR376 |
| D | LEU377 |
| D | THR378 |
| D | GLY379 |
| D | TRP470 |
| D | ZN501 |
| D | MN502 |
| D | BCT504 |
| D | HOH819 |
| D | HOH3344 |
| site_id | CC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN E 501 |
| Chain | Residue |
| E | LYS267 |
| E | ASP272 |
| E | ASP290 |
| E | GLU351 |
| E | MN502 |
| E | BCT504 |
| E | BES505 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN E 502 |
| Chain | Residue |
| E | ASP272 |
| E | ASP349 |
| E | GLU351 |
| E | ZN501 |
| E | BES505 |
| site_id | CC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K E 503 |
| Chain | Residue |
| E | LEU189 |
| E | GLY190 |
| E | LEU192 |
| E | LYS288 |
| E | MET291 |
| E | HOH510 |
| site_id | CC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BCT E 504 |
| Chain | Residue |
| E | LYS267 |
| E | ALA350 |
| E | GLU351 |
| E | GLY352 |
| E | ARG353 |
| E | LEU377 |
| E | ZN501 |
| E | BES505 |
| site_id | CC7 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE BES E 505 |
| Chain | Residue |
| E | LYS267 |
| E | ASP272 |
| E | LYS279 |
| E | MET287 |
| E | ASP290 |
| E | ASP349 |
| E | GLU351 |
| E | THR376 |
| E | LEU377 |
| E | THR378 |
| E | GLY379 |
| E | ALA466 |
| E | TRP470 |
| E | ZN501 |
| E | MN502 |
| E | BCT504 |
| E | HOH1267 |
| E | HOH2741 |
| site_id | CC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN F 501 |
| Chain | Residue |
| F | LYS267 |
| F | ASP272 |
| F | ASP290 |
| F | GLU351 |
| F | MN502 |
| F | BCT504 |
| F | BES505 |
| site_id | CC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MN F 502 |
| Chain | Residue |
| F | ASP272 |
| F | ASP349 |
| F | GLU351 |
| F | ZN501 |
| F | BES505 |
| site_id | DC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K F 503 |
| Chain | Residue |
| F | LEU189 |
| F | GLY190 |
| F | LEU192 |
| F | LYS288 |
| F | MET291 |
| F | HOH518 |
| site_id | DC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BCT F 504 |
| Chain | Residue |
| F | LYS267 |
| F | ALA350 |
| F | GLU351 |
| F | GLY352 |
| F | ARG353 |
| F | LEU377 |
| F | ZN501 |
| F | BES505 |
| site_id | DC3 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE BES F 505 |
| Chain | Residue |
| F | LYS267 |
| F | ASP272 |
| F | LYS279 |
| F | MET287 |
| F | ASP290 |
| F | ASP349 |
| F | GLU351 |
| F | THR376 |
| F | LEU377 |
| F | THR378 |
| F | GLY379 |
| F | ALA466 |
| F | TRP470 |
| F | ZN501 |
| F | MN502 |
| F | BCT504 |
| F | HOH1648 |
Functional Information from PROSITE/UniProt
| site_id | PS00631 |
| Number of Residues | 8 |
| Details | CYTOSOL_AP Cytosol aminopeptidase signature. NTDAEGRL |
| Chain | Residue | Details |
| F | ASN347-LEU354 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255 |
| Chain | Residue | Details |
| F | LYS279 | |
| D | ARG353 | |
| E | LYS279 | |
| E | ARG353 | |
| F | ARG353 | |
| A | LYS279 | |
| A | ARG353 | |
| B | LYS279 | |
| B | ARG353 | |
| C | LYS279 | |
| C | ARG353 | |
| D | LYS279 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 30 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| F | LYS267 | |
| A | GLU351 | |
| B | LYS267 | |
| B | ASP272 | |
| B | ASP290 | |
| B | ASP349 | |
| B | GLU351 | |
| C | LYS267 | |
| C | ASP272 | |
| C | ASP290 | |
| C | ASP349 | |
| F | ASP272 | |
| C | GLU351 | |
| D | LYS267 | |
| D | ASP272 | |
| D | ASP290 | |
| D | ASP349 | |
| D | GLU351 | |
| E | LYS267 | |
| E | ASP272 | |
| E | ASP290 | |
| E | ASP349 | |
| F | ASP290 | |
| E | GLU351 | |
| F | ASP349 | |
| F | GLU351 | |
| A | LYS267 | |
| A | ASP272 | |
| A | ASP290 | |
| A | ASP349 |
