4ZI6
Crystal structure of leucine aminopeptidase from Helicobacter pylori
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 | 0008233 | molecular_function | peptidase activity |
| A | 0008235 | molecular_function | metalloexopeptidase activity |
| A | 0016787 | molecular_function | hydrolase 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 | 0008233 | molecular_function | peptidase activity |
| B | 0008235 | molecular_function | metalloexopeptidase activity |
| B | 0016787 | molecular_function | hydrolase 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 | 0008233 | molecular_function | peptidase activity |
| C | 0008235 | molecular_function | metalloexopeptidase activity |
| C | 0016787 | molecular_function | hydrolase 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 | 0008233 | molecular_function | peptidase activity |
| D | 0008235 | molecular_function | metalloexopeptidase activity |
| D | 0016787 | molecular_function | hydrolase 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 | 0008233 | molecular_function | peptidase activity |
| E | 0008235 | molecular_function | metalloexopeptidase activity |
| E | 0016787 | molecular_function | hydrolase 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 | 0008233 | molecular_function | peptidase activity |
| F | 0008235 | molecular_function | metalloexopeptidase activity |
| F | 0016787 | molecular_function | hydrolase 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 | LYS258 |
| A | ASP263 |
| A | ASP281 |
| A | GLU342 |
| A | ZN502 |
| A | HOH635 |
| A | HOH812 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue ZN A 502 |
| Chain | Residue |
| A | ASP340 |
| A | GLU342 |
| A | ZN501 |
| A | HOH635 |
| A | ASP263 |
| A | LYS270 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue BCT A 503 |
| Chain | Residue |
| A | LYS258 |
| A | ALA341 |
| A | GLU342 |
| A | GLY343 |
| A | ARG344 |
| A | LEU368 |
| A | HOH635 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 504 |
| Chain | Residue |
| A | ALA461 |
| A | GLY462 |
| A | TYR465 |
| A | HOH608 |
| A | HOH652 |
| A | HOH892 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | binding site for residue ZN B 501 |
| Chain | Residue |
| B | LYS258 |
| B | ASP263 |
| B | ASP281 |
| B | GLU342 |
| B | ZN502 |
| B | HOH683 |
| B | HOH721 |
| B | HOH813 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue ZN B 502 |
| Chain | Residue |
| B | ASP263 |
| B | ASP340 |
| B | GLU342 |
| B | ZN501 |
| B | HOH813 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue BCT B 503 |
| Chain | Residue |
| B | LYS258 |
| B | ALA341 |
| B | GLU342 |
| B | GLY343 |
| B | ARG344 |
| B | LEU368 |
| B | HOH813 |
| B | HOH820 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | binding site for residue NA B 504 |
| Chain | Residue |
| B | ALA461 |
| B | GLY462 |
| B | TYR465 |
| B | HOH614 |
| B | HOH674 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | binding site for residue ZN C 501 |
| Chain | Residue |
| C | LYS258 |
| C | ASP263 |
| C | ASP281 |
| C | GLU342 |
| C | ZN502 |
| C | HOH648 |
| C | HOH662 |
| C | HOH848 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue ZN C 502 |
| Chain | Residue |
| C | ASP263 |
| C | ASP340 |
| C | GLU342 |
| C | ZN501 |
| C | HOH648 |
| C | HOH662 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue BCT C 503 |
| Chain | Residue |
| C | LYS258 |
| C | ALA341 |
| C | GLU342 |
| C | GLY343 |
| C | ARG344 |
| C | LEU368 |
| C | HOH648 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue NA C 504 |
| Chain | Residue |
| C | ALA461 |
| C | GLY462 |
| C | TYR465 |
| C | HOH669 |
| C | HOH748 |
| C | HOH869 |
| site_id | AD4 |
| Number of Residues | 8 |
| Details | binding site for residue ZN D 501 |
| Chain | Residue |
| D | LYS258 |
| D | ASP263 |
| D | ASP281 |
| D | GLU342 |
| D | ZN502 |
| D | BCT503 |
| D | HOH698 |
| D | HOH852 |
| site_id | AD5 |
| Number of Residues | 6 |
| Details | binding site for residue ZN D 502 |
| Chain | Residue |
| D | ASP263 |
| D | LYS270 |
| D | ASP340 |
| D | GLU342 |
| D | ZN501 |
| D | HOH698 |
| site_id | AD6 |
| Number of Residues | 8 |
| Details | binding site for residue BCT D 503 |
| Chain | Residue |
| D | ZN501 |
| D | HOH698 |
| D | LYS258 |
| D | ALA341 |
| D | GLU342 |
| D | GLY343 |
| D | ARG344 |
| D | LEU368 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue NA D 504 |
| Chain | Residue |
| D | ALA461 |
| D | GLY462 |
| D | TYR465 |
| D | HOH676 |
| site_id | AD8 |
| Number of Residues | 7 |
| Details | binding site for residue ZN E 501 |
| Chain | Residue |
| E | LYS258 |
| E | ASP263 |
| E | ASP281 |
| E | GLU342 |
| E | ZN502 |
| E | HOH688 |
| E | HOH853 |
| site_id | AD9 |
| Number of Residues | 6 |
| Details | binding site for residue ZN E 502 |
| Chain | Residue |
| E | ASP263 |
| E | ASP340 |
| E | GLU342 |
| E | ZN501 |
| E | HOH688 |
| E | HOH870 |
| site_id | AE1 |
| Number of Residues | 7 |
| Details | binding site for residue BCT E 503 |
| Chain | Residue |
| E | LYS258 |
| E | ALA341 |
| E | GLU342 |
| E | GLY343 |
| E | ARG344 |
| E | LEU368 |
| E | HOH688 |
| site_id | AE2 |
| Number of Residues | 6 |
| Details | binding site for residue NA E 504 |
| Chain | Residue |
| E | ALA461 |
| E | GLY462 |
| E | TYR465 |
| E | HOH624 |
| E | HOH637 |
| E | HOH908 |
| site_id | AE3 |
| Number of Residues | 7 |
| Details | binding site for residue ZN F 501 |
| Chain | Residue |
| F | LYS258 |
| F | ASP263 |
| F | ASP281 |
| F | GLU342 |
| F | ZN502 |
| F | HOH727 |
| F | HOH874 |
| site_id | AE4 |
| Number of Residues | 5 |
| Details | binding site for residue ZN F 502 |
| Chain | Residue |
| F | ASP263 |
| F | ASP340 |
| F | GLU342 |
| F | ZN501 |
| F | HOH727 |
| site_id | AE5 |
| Number of Residues | 7 |
| Details | binding site for residue BCT F 503 |
| Chain | Residue |
| F | LYS258 |
| F | ALA341 |
| F | GLU342 |
| F | GLY343 |
| F | ARG344 |
| F | LEU368 |
| F | HOH727 |
| site_id | AE6 |
| Number of Residues | 4 |
| Details | binding site for residue NA F 504 |
| Chain | Residue |
| F | ALA461 |
| F | GLY462 |
| F | TYR465 |
| F | HOH614 |
Functional Information from PROSITE/UniProt
| site_id | PS00631 |
| Number of Residues | 8 |
| Details | CYTOSOL_AP Cytosol aminopeptidase signature. NTDAEGRL |
| Chain | Residue | Details |
| A | ASN338-LEU345 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 30 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
