2HPT
Crystal Structure of E. coli PepN (Aminopeptidase N)in complex with Bestatin
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 | BES960 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE BES A 960 |
| Chain | Residue |
| A | HIS297 |
| A | GLU298 |
| A | HIS301 |
| A | LYS319 |
| A | GLU320 |
| A | ASN373 |
| A | TYR376 |
| A | TYR381 |
| A | ZN950 |
| A | HOH1611 |
| A | HOH1695 |
| A | GLU121 |
| A | MET260 |
| A | GLY261 |
| A | ALA262 |
| A | GLU264 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL A 971 |
| Chain | Residue |
| A | SER63 |
| A | VAL64 |
| A | TRP71 |
| A | THR72 |
| A | TRP74 |
| A | ARG669 |
| A | VAL670 |
| A | GLU671 |
| A | HOH1092 |
| A | HOH1201 |
| A | HOH1531 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 972 |
| Chain | Residue |
| A | LEU532 |
| A | TRP546 |
| A | ASP566 |
| A | SER570 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 973 |
| Chain | Residue |
| A | THR72 |
| A | TRP74 |
| A | VAL670 |
| A | GLU671 |
| A | HOH1440 |
| A | HOH1531 |
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 |
