4XN2
Crystal Structure of Met260Ala mutant of E. coli Aminopeptidase N in complex with L-Leucine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004177 | molecular_function | aminopeptidase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0006508 | biological_process | proteolysis |
| A | 0008233 | molecular_function | peptidase activity |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0016285 | molecular_function | alanyl aminopeptidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue ZN A 901 |
| Chain | Residue |
| A | HIS297 |
| A | HIS301 |
| A | GLU320 |
| A | LEU902 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue LEU A 902 |
| Chain | Residue |
| A | GLU298 |
| A | HIS301 |
| A | LYS319 |
| A | GLU320 |
| A | TYR376 |
| A | TYR381 |
| A | ZN901 |
| A | HOH1441 |
| A | GLN119 |
| A | GLU121 |
| A | ALA262 |
| A | GLU264 |
| A | HIS297 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 903 |
| Chain | Residue |
| A | SER332 |
| A | ASP333 |
| A | GLY335 |
| A | HOH1594 |
| A | HOH1680 |
| A | HOH1843 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 904 |
| Chain | Residue |
| A | ASP452 |
| A | GOL915 |
| A | HOH1614 |
| A | HOH1729 |
| A | HOH1809 |
| A | HOH1816 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 905 |
| Chain | Residue |
| A | GLU426 |
| A | ASP432 |
| A | SER434 |
| A | HOH1491 |
| A | HOH1822 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 906 |
| Chain | Residue |
| A | SER48 |
| A | LEU86 |
| A | HOH1045 |
| A | HOH1588 |
| A | HOH1664 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 907 |
| Chain | Residue |
| A | THR347 |
| A | HOH1359 |
| A | HOH1679 |
| A | HOH1832 |
| A | HOH1845 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 908 |
| Chain | Residue |
| A | GLU371 |
| A | HOH1009 |
| A | HOH1083 |
| A | HOH1123 |
| A | HOH1252 |
| A | HOH1813 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 909 |
| Chain | Residue |
| A | GLN19 |
| A | ILE20 |
| A | LEU138 |
| A | HOH1580 |
| A | HOH1819 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 910 |
| Chain | Residue |
| A | TYR185 |
| A | GLU264 |
| A | GLY305 |
| A | ASN306 |
| A | LYS319 |
| site_id | AD2 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 911 |
| Chain | Residue |
| A | GLY350 |
| A | ASN623 |
| A | GLU627 |
| A | HOH1341 |
| A | HOH1659 |
| A | HOH1744 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 912 |
| Chain | Residue |
| A | ARG293 |
| A | ASN344 |
| A | HOH1096 |
| A | HOH1100 |
| A | HOH1456 |
| A | HOH1832 |
| site_id | AD4 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 913 |
| Chain | Residue |
| A | HIS771 |
| A | PHE774 |
| A | HOH1144 |
| A | HOH1524 |
| A | HOH1759 |
| site_id | AD5 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 914 |
| Chain | Residue |
| A | ARG641 |
| A | THR645 |
| A | ARG686 |
| A | PHE690 |
| A | ALA722 |
| A | HOH1129 |
| A | HOH1297 |
| A | HOH1394 |
| site_id | AD6 |
| Number of Residues | 12 |
| Details | binding site for residue GOL A 915 |
| Chain | Residue |
| A | ASP452 |
| A | TYR544 |
| A | LYS545 |
| A | GLN550 |
| A | NA904 |
| A | HOH1059 |
| A | HOH1165 |
| A | HOH1266 |
| A | HOH1437 |
| A | HOH1614 |
| A | HOH1729 |
| A | HOH1761 |
| site_id | AD7 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 916 |
| Chain | Residue |
| A | LYS274 |
| A | TYR275 |
| A | ARG783 |
| A | ARG825 |
| A | HOH1292 |
| A | HOH1866 |
| A | ALA260 |
| A | GLY261 |
| site_id | AD8 |
| Number of Residues | 4 |
| Details | binding site for residue MLI A 917 |
| Chain | Residue |
| A | ARG728 |
| A | ASP729 |
| A | MET732 |
| A | GLN753 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue MLI A 918 |
| Chain | Residue |
| A | GLN587 |
| A | PRO588 |
| A | LEU589 |
| A | ALA643 |
Functional Information from PROSITE/UniProt
| site_id | PS00142 |
| Number of Residues | 10 |
| Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VIGHEYFHNW |
| Chain | Residue | Details |
| A | VAL294-TRP303 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"16885166","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"18416562","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"19622865","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
