4XNA
Crystal Structure of E. coli Aminopeptidase N in complex with L-Beta Homolysine
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 | B3K902 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | binding site for residue B3K A 902 |
| Chain | Residue |
| A | GLU298 |
| A | HIS301 |
| A | LYS319 |
| A | GLU320 |
| A | ASN373 |
| A | TYR376 |
| A | TYR381 |
| A | GLN821 |
| A | ZN901 |
| A | MLI920 |
| A | HOH1129 |
| A | HOH1219 |
| A | GLU121 |
| A | ALA262 |
| A | MET263 |
| A | GLU264 |
| A | HIS297 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 903 |
| Chain | Residue |
| A | GLN19 |
| A | ILE20 |
| A | LEU138 |
| A | HOH1390 |
| A | HOH1687 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 904 |
| Chain | Residue |
| A | SER332 |
| A | ASP333 |
| A | GLY335 |
| A | HOH1301 |
| A | HOH1530 |
| A | HOH1532 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue NA A 905 |
| Chain | Residue |
| A | TYR185 |
| A | GLU264 |
| A | GLY305 |
| A | ASN306 |
| A | LYS319 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 906 |
| Chain | Residue |
| A | LEU551 |
| A | SER570 |
| A | THR574 |
| A | HOH1338 |
| A | HOH1358 |
| A | HOH1692 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 907 |
| Chain | Residue |
| A | ALA531 |
| A | LEU532 |
| A | TRP546 |
| A | ASP566 |
| A | ALA567 |
| A | SER570 |
| A | HOH1031 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 908 |
| Chain | Residue |
| A | LEU289 |
| A | SER336 |
| A | HIS672 |
| A | ILE675 |
| A | HOH1250 |
| A | HOH1293 |
| A | HOH1312 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 909 |
| Chain | Residue |
| A | ASN67 |
| A | ASP68 |
| A | THR91 |
| A | HOH1055 |
| A | HOH1533 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 910 |
| Chain | Residue |
| A | ASP452 |
| A | GLN527 |
| A | PRO528 |
| A | HOH1022 |
| A | HOH1041 |
| site_id | AD2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 911 |
| Chain | Residue |
| A | LEU61 |
| A | VAL62 |
| A | TRP74 |
| A | ARG669 |
| A | GLU671 |
| A | GOL915 |
| A | HOH1094 |
| site_id | AD3 |
| Number of Residues | 11 |
| Details | binding site for residue GOL A 912 |
| Chain | Residue |
| A | PRO179 |
| A | PHE180 |
| A | PRO181 |
| A | ARG307 |
| A | ASP412 |
| A | GLY413 |
| A | PRO592 |
| A | VAL593 |
| A | HIS594 |
| A | HOH1006 |
| A | HOH1476 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 913 |
| Chain | Residue |
| A | LYS501 |
| A | PHE519 |
| A | VAL520 |
| A | HOH1381 |
| site_id | AD5 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 914 |
| Chain | Residue |
| A | PRO16 |
| A | ASP17 |
| A | TYR18 |
| A | PRO51 |
| A | LEU52 |
| A | ARG53 |
| A | LEU132 |
| A | ARG134 |
| A | HOH1001 |
| A | HOH1085 |
| site_id | AD6 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 915 |
| Chain | Residue |
| A | VAL64 |
| A | TRP71 |
| A | THR72 |
| A | TRP74 |
| A | ARG669 |
| A | VAL670 |
| A | GLU671 |
| A | GOL911 |
| A | HOH1302 |
| A | HOH1406 |
| site_id | AD7 |
| Number of Residues | 8 |
| Details | binding site for residue MLI A 916 |
| Chain | Residue |
| A | ARG641 |
| A | GLU642 |
| A | THR645 |
| A | ARG686 |
| A | PHE690 |
| A | ALA722 |
| A | HOH1056 |
| A | HOH1145 |
| site_id | AD8 |
| Number of Residues | 5 |
| Details | binding site for residue MLI A 917 |
| Chain | Residue |
| A | ASP281 |
| A | ASN709 |
| A | LYS738 |
| A | TRP739 |
| A | HOH1175 |
| site_id | AD9 |
| Number of Residues | 10 |
| Details | binding site for residue MLI A 918 |
| Chain | Residue |
| A | HIS11 |
| A | ARG14 |
| A | GLN467 |
| A | ARG468 |
| A | THR469 |
| A | LYS478 |
| A | GLN479 |
| A | PRO480 |
| A | ALA515 |
| A | HOH1191 |
| site_id | AE1 |
| Number of Residues | 5 |
| Details | binding site for residue MLI A 919 |
| Chain | Residue |
| A | GLU671 |
| A | HIS672 |
| A | HOH1003 |
| A | HOH1094 |
| A | HOH1363 |
| site_id | AE2 |
| Number of Residues | 8 |
| Details | binding site for residue MLI A 920 |
| Chain | Residue |
| A | MET260 |
| A | GLY261 |
| A | ALA262 |
| A | ARG293 |
| A | VAL294 |
| A | TYR381 |
| A | B3K902 |
| A | HOH1021 |
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 |
