1ONW
Crystal structure of Isoaspartyl Dipeptidase from E. coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006508 | biological_process | proteolysis |
| A | 0008237 | molecular_function | metallopeptidase activity |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0008798 | molecular_function | beta-aspartyl-peptidase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006508 | biological_process | proteolysis |
| B | 0008237 | molecular_function | metallopeptidase activity |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0008798 | molecular_function | beta-aspartyl-peptidase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 800 |
| Chain | Residue |
| A | HIS68 |
| A | HIS70 |
| A | KCX162 |
| A | ASP285 |
| A | ZN801 |
| A | HOH841 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 801 |
| Chain | Residue |
| A | HIS230 |
| A | ZN800 |
| A | HOH841 |
| A | TYR137 |
| A | KCX162 |
| A | HIS201 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 802 |
| Chain | Residue |
| B | HIS68 |
| B | HIS70 |
| B | KCX162 |
| B | ASP285 |
| B | ZN803 |
| B | HOH864 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 803 |
| Chain | Residue |
| B | TYR137 |
| B | KCX162 |
| B | HIS201 |
| B | HIS230 |
| B | ZN802 |
| B | HOH864 |
| site_id | AC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MG B 804 |
| Chain | Residue |
| B | HOH978 |
| B | HOH978 |
| B | HOH979 |
| B | HOH979 |
| B | HOH991 |
| B | HOH991 |
| B | HOH1003 |
| B | HOH1003 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE NA B 805 |
| Chain | Residue |
| A | HOH886 |
| B | GLY193 |
| B | EDO807 |
| B | HOH869 |
| B | HOH998 |
| B | HOH1052 |
| B | HOH1107 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 802 |
| Chain | Residue |
| A | LEU89 |
| A | GLY385 |
| A | HOH918 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 806 |
| Chain | Residue |
| B | ALA88 |
| B | LEU89 |
| B | GLY385 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 803 |
| Chain | Residue |
| A | ASP167 |
| A | HIS168 |
| A | ASP204 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 804 |
| Chain | Residue |
| A | ALA153 |
| A | LEU191 |
| A | HOH839 |
| A | HOH964 |
| B | ALA118 |
| B | ARG121 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO A 805 |
| Chain | Residue |
| A | LEU117 |
| A | ALA118 |
| A | ARG121 |
| A | HOH848 |
| A | HOH970 |
| B | ALA153 |
| B | LEU191 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 807 |
| Chain | Residue |
| B | TRP131 |
| B | GLY193 |
| B | PRO195 |
| B | ASN341 |
| B | LEU342 |
| B | NA805 |
| B | HOH869 |
| B | HOH989 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:12946361 |
| Chain | Residue | Details |
| A | ASP285 | |
| B | ASP285 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12718528, ECO:0000269|PubMed:12946361, ECO:0000269|PubMed:15882050, ECO:0000269|PubMed:16289685 |
| Chain | Residue | Details |
| A | HIS68 | |
| B | ASP285 | |
| A | HIS70 | |
| A | HIS201 | |
| A | HIS230 | |
| A | ASP285 | |
| B | HIS68 | |
| B | HIS70 | |
| B | HIS201 | |
| B | HIS230 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLY75 | |
| B | GLY75 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:12718528, ECO:0000305|PubMed:12946361, ECO:0000305|PubMed:15882050 |
| Chain | Residue | Details |
| A | THR106 | |
| B | SER289 | |
| A | TYR137 | |
| A | ARG169 | |
| A | ARG233 | |
| A | SER289 | |
| B | THR106 | |
| B | TYR137 | |
| B | ARG169 | |
| B | ARG233 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: via carbamate group => ECO:0000269|PubMed:12718528, ECO:0000269|PubMed:12946361, ECO:0000269|PubMed:15882050, ECO:0000269|PubMed:16289685 |
| Chain | Residue | Details |
| A | KCX162 | |
| B | KCX162 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-carboxylysine => ECO:0000269|PubMed:12718528, ECO:0000269|PubMed:12946361, ECO:0000269|PubMed:15882050, ECO:0000269|PubMed:16289685 |
| Chain | Residue | Details |
| A | KCX162 | |
| B | KCX162 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 172 |
| Chain | Residue | Details |
| A | HIS68 | metal ligand |
| A | HIS70 | metal ligand |
| A | KCX162 | metal ligand |
| A | HIS201 | metal ligand |
| A | HIS230 | metal ligand |
| A | ASP285 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 172 |
| Chain | Residue | Details |
| B | HIS68 | metal ligand |
| B | HIS70 | metal ligand |
| B | KCX162 | metal ligand |
| B | HIS201 | metal ligand |
| B | HIS230 | metal ligand |
| B | ASP285 | hydrogen bond acceptor, hydrogen bond donor, metal ligand, proton acceptor, proton donor |
