4XN9
Crystal Structure of E. coli Aminopeptidase N in complex with Beta Alanine
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 | BAL902 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue BAL A 902 |
Chain | Residue |
A | GLU298 |
A | HIS301 |
A | LYS319 |
A | GLU320 |
A | TYR381 |
A | ZN901 |
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 | SER332 |
A | ASP333 |
A | GLY335 |
A | HOH1173 |
A | HOH1229 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue NA A 904 |
Chain | Residue |
A | GLN19 |
A | ILE20 |
A | LEU138 |
A | HOH1187 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue MLI A 905 |
Chain | Residue |
A | LEU532 |
A | LEU554 |
A | ASP566 |
A | ALA567 |
A | SER570 |
A | HOH1030 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue MLI A 906 |
Chain | Residue |
A | ARG161 |
A | ARG198 |
A | GLU212 |
A | TYR214 |
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 |