4XN1
Crystal Structure of Met260Ala mutant of E. coli Aminopeptidase N in complex with L-Glutamate
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 | GLU902 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue GLU A 902 |
| Chain | Residue |
| A | GLU298 |
| A | HIS301 |
| A | GLU320 |
| A | TYR381 |
| A | ZN901 |
| A | NA904 |
| A | HOH1002 |
| A | HOH1046 |
| A | HOH1056 |
| A | HOH1062 |
| A | HOH1489 |
| A | ALA260 |
| A | GLY261 |
| 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 | HOH1486 |
| A | HOH1700 |
| A | HOH1739 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 904 |
| Chain | Residue |
| A | GLU121 |
| A | GLU264 |
| A | LYS319 |
| A | GLU320 |
| A | GLU902 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 905 |
| Chain | Residue |
| A | GLY350 |
| A | ASN623 |
| A | GLU627 |
| A | HOH1148 |
| A | HOH1348 |
| A | HOH1857 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 906 |
| Chain | Residue |
| A | MLI914 |
| A | HOH1052 |
| A | HOH1249 |
| A | HOH1662 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 907 |
| Chain | Residue |
| A | ASP24 |
| A | LEU25 |
| A | THR26 |
| A | THR37 |
| A | HOH1872 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue NA A 908 |
| Chain | Residue |
| A | GLU121 |
| A | ASN373 |
| A | GLN821 |
| A | HOH1011 |
| A | HOH1654 |
| A | HOH1669 |
| A | HOH1768 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 909 |
| Chain | Residue |
| A | GLU77 |
| A | ALA80 |
| A | TYR130 |
| A | HOH1241 |
| A | HOH1734 |
| site_id | AD1 |
| Number of Residues | 4 |
| Details | binding site for residue NA A 910 |
| Chain | Residue |
| A | GLU371 |
| A | HOH1017 |
| A | HOH1063 |
| A | HOH1140 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 911 |
| Chain | Residue |
| A | TYR185 |
| A | GLU264 |
| A | GLY305 |
| A | ASN306 |
| A | LYS319 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 912 |
| Chain | Residue |
| A | GLN569 |
| A | LEU572 |
| A | GLU615 |
| A | ILE616 |
| A | THR618 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue MLI A 913 |
| Chain | Residue |
| A | PHE704 |
| A | GLU734 |
| A | TYR735 |
| A | LYS738 |
| A | TRP739 |
| A | HOH1085 |
| site_id | AD5 |
| Number of Residues | 11 |
| Details | binding site for residue MLI A 914 |
| Chain | Residue |
| A | LEU289 |
| A | GLY335 |
| A | SER336 |
| A | VAL339 |
| A | ASN340 |
| A | HIS672 |
| A | ALA676 |
| A | NA906 |
| A | HOH1042 |
| A | HOH1098 |
| A | HOH1232 |
| site_id | AD6 |
| Number of Residues | 4 |
| Details | binding site for residue MLI A 915 |
| Chain | Residue |
| A | GLY396 |
| A | GLU397 |
| A | GLU398 |
| A | HOH1144 |
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 |
