3B3B
Crystal structure of E. coli Aminopeptidase N in complex with tryptophan
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 950 |
| Chain | Residue |
| A | HIS297 |
| A | HIS301 |
| A | GLU320 |
| A | TRP900 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE NA A 951 |
| Chain | Residue |
| A | HOH1502 |
| A | SER332 |
| A | ASP333 |
| A | GLY335 |
| A | HOH1119 |
| A | HOH1265 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE NA A 952 |
| Chain | Residue |
| A | ASP452 |
| A | HOH1506 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE TRP A 900 |
| Chain | Residue |
| A | GLN119 |
| A | GLU121 |
| A | MET260 |
| A | ALA262 |
| A | MET263 |
| A | GLU264 |
| A | HIS297 |
| A | GLU298 |
| A | HIS301 |
| A | LYS319 |
| A | GLU320 |
| A | ASN373 |
| A | TYR376 |
| A | TYR381 |
| A | GLN821 |
| A | HOH1111 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MLI A 990 |
| Chain | Residue |
| A | GLY261 |
| A | TYR275 |
| A | ARG783 |
| A | ARG825 |
| A | HOH1657 |
| A | HOH1820 |
| A | HOH1834 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 970 |
| Chain | Residue |
| A | LEU532 |
| A | TRP546 |
| A | SER563 |
| A | ASP566 |
| A | ALA567 |
| A | SER570 |
| A | HOH1771 |
| A | HOH1793 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 971 |
| Chain | Residue |
| A | SER63 |
| A | TRP71 |
| A | TRP74 |
| A | ARG669 |
| A | GLU671 |
| A | HOH1091 |
| A | HOH1709 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 972 |
| Chain | Residue |
| A | ARG681 |
| A | GLN703 |
| A | ALA707 |
| A | ASN708 |
| A | ASN709 |
| A | ASP712 |
| A | HOH1289 |
| A | HOH1297 |
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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1h19 |
| Chain | Residue | Details |
| A | GLU264 | |
| A | GLU298 | |
| A | TYR381 |
